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THE ROLES OF AMINO ACID CHELATES IN ANIMAL NUTRITION THE ROLES OF AMINO ACID CHELATES IN ANIMAL NUTRITION Edited by H DeWayne Ashmead Albion Laboratories, Inc Clearfield, Utah Reprint Edition NOYES PUBUCATIONS Westwood, New Jersey, U.S.A Copyright © 1993 by Noyes Publications No part of this book may be reproduced or utilized in any form or by any means, electronic or mechanical, including photocopying, recording or by any information storage and retrieval system, without permission in writing from the Publisher Library of Congress Catalog Card Number: 92-25242 ISBN: 0-8155-1312-7 Printed in the United States Published in the United States of America by Noyes Publications Fairview Avenue, Westwood, New Jersey 07675 1098 432 Library of Congress Cataloging-in-Publication Data The Roles of amino acid chelates in animal nutrition / edited by H DeWayne Ashmead p em Includes bibliographical references (p ) and indexes ISBN 0-8155-1312-7 Amino acid chelates in animal nutrition Ashmead, H DeWayne 1992 SF98.A38R64 636.08'52 dc20 92-25242 CIP INTRODUCTION Th i s book wi 11 be of great interest to anyone concerned with animal feeds and feeding programs whether one is studying bovine, porcine, equine, avian or lower vertebrate (fish and eel) nutrition This information is critical to the success of an animal feeding program Somet imes the di fference between a successful and a failing program can be traced to mineral deficiencies which cause either abnormal growth, reduced milk production, interrupted fertility and breeding, compromised immune system integrity and/or decrement in normal hemoglobin concentration Increased morbidity/mortality rates can make a profitable animal feeding program into a financial failure overnight when the replacement costs for a prize animal are considered These abnormalities, and others, are addressed in the pages that follow From 25 controlled studies by 42 different authors in five different countries a diverse array of data is presented These data val i date the effect i veness of mineral nutrients presented as amino acid chelates when compared with the ionic forms derived from the inorganic sal ts These stud i es further support the resul ts of numerous laboratory experiments showing increased absorption, assimilation and reduced toxicity of the forms of minerals chelated to amino acids With little cost and effort animals can be supplemented with amino acid chelates which will promote, with little risk of overdose, a fuller genetic potential achievement as far as mineral requirements are concerned Results of this supplementation are reflected in increased growth, immunological integrity, and more consistent reproduction (increased ovulation and conception after first service) as a result of increased bioavailability of these chelated forms v VI Introduction Of novel interest are the reports showing a protein sparing as a result of amino acid chelate supp1ementat ion In the face of dwi ndl i ng protei n sources for animal feeds, this effect of chelated minerals needs further scrutiny in feeding programs in other species Darrell J Graff, Ph.D Weber State University Ogden, Utah, U.S.A A NOTE TO THE READER In the late 1800's, many of the fundamental concepts of che 1at ion chemi stry were evo 1vi ng Chemi sts began to recognize that certain atoms could exist in more than one valence state, but could not comprehend how atoms with more than one valence could form a highly stable compound Alfred Werner, a German chemist, was the first to break with traditional thinking and propose an entirely new molecular structure to describe these highly stable molecules He noted that certain structural entities, which he called "complexes", remained intact through a series of chemical transformations In 1893, Werner wrote, "If we think of the metal ion as the center of the whole system, then we can most simply place the mo 1ecul es bound to it at the corners of an octahedron."(1) For the first time a chelate had been described Werner further refined this revolutionary concept in the succeeding years He concluded that a metal ion was characterized by two valences The first, which he called the "principal valency", is now termed the oxidation state, or oxidation number, of the metal The second valency, which he called the "auxiliary valency", represents the number of ligand atoms associated with This is the same as the the central metal atom Werner's concepts coord i nat i on number of the metal were fundamental to the comprehension of chelates (2-7) The term, "chelate", was finally used by Morgan and Drew, in 1920, to describe the molecular structure discovered by Werner As noted above, the fi rst chelating molecules that had been discovered were those VII VIII A Note to the Reader with two points of attachment It was this caliper-like mode of attaching the ligand (the chelating molecule) to the metal atom that led Morgan and Drew to suggest the word "chelate" to describe the molecule.(8) The word is derived from the Greek word "chele", meaning lobster's claw The word, IIchelate was originally used as an adjective It later became a more versatile word and today i s used as an adj ect i ve, adverb, or noun The ligands are chelating agents, and the complexes they form are metal chelates ll , Because the claw, or ligand, held the cation, the metal was no longer free to enter into other chemical reactions Thus it quickly became evident that when a metal was che1ated, the chemi cal and phys i cal characteristics of the constituent metal ion and ligands were changed This had far reaching consequences in the realms of chemistry and general biology In spite of the knowledge of what chelation could to and for a metal ion, it was not until the early 1960's that anyone thought seriously about using this molecule for nutritional purposes At that period, a handful of investigators, independent of each other, each conceived the idea that if a metal ion could be chelated before feeding it to animals, the ligand would sequester the cation and prevent it from entering into various absorption inhibiting chemical reactions in the gut The theoretical consequence was greater nutritional uptake of the ions Two schools of thought quickly developed One, led by the pioneering research of Albion Laboratories, Inc., proposed that amino acid chelates were the proper chelates to enhance mineral absorption As attested by a large number of research reports, lectures, and publications based on the research efforts both A Note to the Reader IX coordinated and conducted by this organization, the use of amino acid chelates in animal nutrition were both positive and highly encouraging At that point in time these amino acids were called "metal proteinates" instead of chelates Concurrently, with the development of the amino acid chelates, a second school of thought approached animal nutrition with synthetic chelates based on ethylenediaminetetraacetic acid (EOTA) The theory was the same as before The EOTA ligand would chelate the cation and protect it from chemical reactions in the gut While it successfully accomplished its mission in terms of protect ion, it genera11 y fa i 1ed to enhance mineral nutrition because it formed chelates that were too stable The biological ligands in the animals' bodies were incapable of extracting the cations from the EOTA chelates, even after they were absorbed into the blood Thus, the EOTA chelates were returned to the lower bowels or excreted into the urine still protecting the cations that the animal s were supposed to have utilized As Bates, et li., concluded, even though chelation plays a dominant role in mineral absorption, "chelation does not, in itself, insure efficient uptake because the absorption of the ferric chelates of EOTA, NTA, and gluconate were not significantly different than that of ferrous sul fate ,,(9) These synthetic chelates were heavily promoted in the decade of the 60's and the early part of the 70's When they could not deliver the enhanced mineral nutrition promised by the chelation concept, all nutritional products using the word "chelation" lost favor with most animal nutritionists The "c" word became a word to avoid if one wished to amicably discuss animal nutrition Summary and Conclusion 465 acid chelate must have a molecular weight of less than 1,500 da1 0ns to initially comply for intact absorption 2) Similarity to molecules recognized by specific carriers also plays a part in the improved bioavailability of the amino acid chelates as in the case of dipeptide and tripeptide-like chelates being similar to the small peptides which the mucosal cell is already accustomed to Larger molecules require digestion before absorption, and digestion results in a loss of the chelate benefits Once absorbed, the fate of the amino acid chelate is varied Because the amino acid chelate is a selfcontained and protected organic molecule which is compatible with biological processes, it can be transferred, intact, into tissues and enter into many metabolic processes without further degradation This is very evident in cases of amino acid chelates being given to gestating animals The amino acid chelated mineral are transferred across the placenta and into the fetus as intact molecules, because their size and form is compatible with other small molecules which are likewise, not impeded (i.e sugars, amino acids, etc.) The result is the offspring are born with higher tissue mineral levels, including(hjgher hemoglobi? levels, when iron amino acid chelates 13 are provided 11) The delivery of greater quantities of a particular mineral to specific sites in the body is also evidence of this intact absorption and translocation of the amino acid chelates Since minerals are utilized as essential enzyme cofactors in many necessary systems of the body, the resul ts of thi s predi spos it i on to greater absorpt ion are evident in the marked improvements of those systems To illustrate, an enhanced immune response has been demonstrated when an~mrls diets were supplemented with amino acid chelates 12 In another study, it was noted that problems with infertility were significantly reduced by providin~ pietary supplements containing amino acid chelates 13 In all of these above cited 466 The Roles of Amino Acid Chelates in Animal Nutrition cases as well as others included in this book, the higher deposition of the supplemented minerals within the targeted tissue necess i tated that the ami no ac id chelates be maintained as intact molecules in order to effect the transfer rather then being broken and having their metal components bound by standard transfer agents in the body The exact mechanism for the transfer of a large quantity of a specific amino acid chelate to a target tissue has not yet been defined Nevertheless, when equivalent amounts of metal salts are administered, that portion which is absorbed is diffused throughout the body and not concentrated in a specific tissue as can occur with the amino acid chelate The amino acid che1ate, therefore responds to a separate and un i que metabolism which is different from that of absorbed free metal cations Besides being utilized as an intact amino acid chelate, degradation of the chelate to the amino acid ligands and the metal can occur in the tissue of usage Anderson demonstrated, while working with iron chelates, that the iron binding capacity in ~ was considerably different from that in vitro Consequently degradation models developed in vitro may not be applicable in the animal For example, in vitro certain che1ates no degrade But once absorbed they are metabolized and function differently than in vitro models would predict This concept is clearly demonstrated in numerous studies where feed conversion rates are enhanced, and where greater weight gains are achieved In these cases, the amino acid chelate was absorbed and subsequently delivered the mineral into the body Degradation occurred at the point where needed, with the mineral from the absorbed amino acid chelate bei ng incorporated into enzyme systems essent i a1 to effect move immediate changes in the animal's metabolism These metabolic changes in the animal could not have occurred if the chelate had not degraded thus allowing the metal to become a co-factor in a specific enzyme necessary to accomplish that metabolic function Summary and Conclusion 467 The degradation of the absorbed amino acid chelate is probably due to a higher stabi 1i ty constant for the ligand portion of the enzyme which requires the metal cation that the stability constant of the original absorbed amino acid chelate In the cells of the body, the stability constant of the amino acid chelate is frequent 1y mod i fi ed by changes in pH as the che1ate migrates a1rRss the membranes of the cell and its organelles 22 A pH change in the environment where a specific enzyme ligand requires a cation could induce the amino acid ligand to donate its cation and degrade intracellularly There are millions of ligand molecules in an animal's body The absorbed minerals are found attached to one, two, or many ligands (within the limits of sterochemistry) in order to create the biological When systems essent i al for the 1i fe process functioning in enzymes, which is generally where the nutritionist sees the most radical changes in animal performance as a result of mineral supplementation, the absorbed mi nera1s become part of meta11 oenzymes and metal-act i vated enzymes The metal and the protei n (which functions as the ligand) are covalently combined in the metalloenzymes Enzymatic activity is lost or retarded when the metal is experimentally removed from the protei n In the case of the metal act i vated enzymes, the metal and the protein ligand are reversibly combined In that situation, one metal may be replaced by certain other metals which ~il~ block, accelerate or retard the enzymatic activity 15 Since these metal-conta in i ng enzymes represent ultra-efficient biological catalysts that are produced within living systems, the feeding of highly available amino acid chelates generally results in greater enzrm~ synthesis and, hence greater enzymatic activity 16 This results in significantly enhanced performance from the animals 468 The Roles of Amino Acid Che/ates in Animal Nutrition The bodies of animals also contain millions of other unique protein molecules, besides those used for enzymes, all of which are excellent ligands for metal The primary structure is probably the ions These protein molecules form ternary polypeptide compl exes wi th the metal s then conferri ng enzymat i c activity and becoming involved in the transport and storage of other biologically active molecules Increased superoxide di smutase act i vi ty is one such benefit rTs~lting from the intake of certain amino acid chelates 17 Normally, one would anticipate that greater absorption of the mineral equates to greater potential for toxicity Toxicity is, to a degree, a function of In 1etha1 dose the 1i gand that bi nds the mi nera1 studies, it was found that the amino acid chelates were significantly less toxic than 1o~responding amounts of Long term, multimetals in the form of salts 19 generation histopathological studies with amino acid chelates produced ?o)abnormalities in the tissues of the Thus, within the context of animals examined 20 nutritive practices, the amino acid chelates are considered a safe source of highly available minerals In summary, Kratzer and Vohra wrote, "the dietary requirement for a mineral may be greatly reduced by the addition of a chelating agent to a diet A practical quest ion ari ses about whether one shoul d correct a marginal mineral deficiency in a diet by adding the mineral [as a salt], a chelate [as a ligand], or a chelated mineral While it might be possible to use the chelate, or chelated mineral, it is a matter of relative costs that will influence the decision In most cases, the cost of the mineral supplement itself( i~ less than that of the che1ate or che1ated mi nera1." 21 The observations of these two professors is correct, and as the data contained within this book demonstrate, if the decision to use amino acid chelates Summary and Conclusion 469 or metal salts in animal feeds is based on a complete assessment of economics, the decision must result in Based on the choosing the amino acid chelates statistically analyzed animal performances, reported in the pages of this book, the return on investment is far greater wi th the ami no ac id che1ates when than for comparable metal salts Supplementing with amino acid chelates is more cost effective, yielding greater profits per unit spent 470 The Roles of Amino Acid Chelates in Animal Nutrition References Morgan, G and Drew, H., "Researches on residual affinity and coordination II Acetylacetones of selenium and tellurium," J Chern Soc., 117:1456, 1920 Ashmead, H D., et ~., Intestinal Absorption of Metal Ions and Chelates (Springfield: Charles C Thomas) 1985 Mellor, D., "Historical background and fundamental concepts," in Dweyer, F and Mellor, D., eds., Chelating Agents and Metal Chelates (New York: Academic Press) 1-50, 1964 Kragten, J., Atlas of Metal - Ligand Equilibria in Aqueous Solution (Chichester: Ellis Horwood Ltd) 1978 Seven, J., ed., Metal Binding in Medicine (Philadelphia: J B Lippincott Co) 1960 Vohra, P and Kratzer, F., "Influence of various chelating agents on the availability of zinc," J Nutr., 82:249, 1964 Miller, R., "Chelating agents in poultry nutrition," Presented at Delmarva Nutrition Short Course, 1968 Miller, J., "Chelation", privately printed, 1960 Ashmead, H., et ~., "Chel ation does not guarantee mineral metabolism," J Appl Nutr., 26:7, Summer, 1974 Summary and Conclusion 471 10 Ashmead, H D., IIA peptide dependent intestinal pathway for the absorption of essential minerals,1I in Southgate, D., et li., eds., Nutrient Availability: Chemical and Biological Aspects (Cambridge: The Royal Chemical Society) 123, 1989 11 Ashmead, D and Graff, D., "Placental transport of chelated iron,1I Proc Int Pig Vet Soc Congress, Mexico, 207, 1982 12 Coffey, R., "Predisposition to disease: The inter-relationship of the bovine immune response and trace element physiology," Paper given at National Cattleman Assoc., 1986 13 Manspeaker, J., et li., "Chelated minerals: Their role in bovine fertility," Vet Med., 82:951, 1987 14 Anderson, W., IIIron chelation in the treatment of Csoley's anemia," in Martell, A., ed., Inorganic Chemistry in Biology and Medicine (Washington D.C.: American Chemical Society) 140, 1980 15 Schuette, K., The Biology of the Trace Elements (Philadelphia: J B Lippincott Co.) 17, 1964 16 Maletto, S., "Studies on the nourishing action model in the protalosates," Unpublished, 1982 17 Coffey, R., et li., "Clinical data on immunoglobulin serum levels, trace elements in feedstuffs and liver copper levels in clinically ill cattle," Unpublished, 1982-1985 18 Williams, D., The Metals of Life (London: Van Nostrand Reinhold) 1971 472 The Roles of Amino Acid Chelates in Animal Nutrition 19 Larson, A., "L.D 50 Studies with Chelated Minerals," in Ashmead, D., ed., Chelated Mineral Nutrition in Plants, Animals, and Man (Springfield: Charles C Thomas) 163, 1982 20 Jeppsen, R., "Assessment of long-term feeding of chelated amino acid minerals (Metalosates@) in sows), Unpublished, 1987 21 Kratzer, F and Vohra, P., Chelates in Nutrition (Boca Raton: CRC Press, Inc.) 158, 1986 NAME INDEX A ~bion Iowa Sta1e ~iversity, 216, 217 Iwahasi, Yoshito, 440 Laboratories, Inc., X, 86, 106, 107, 207, 457 Ash~,H.DeVVayne,21,47,207,457 Ash~, J Harvey H., 413 ~, ~, 269, 291, 380 J Bibby Agricultural LTD., 274 B Jeppsen, Robert B., 106 Biti, R Ricci, 243 Boling, James A, 187 BoIsi, Dan iel Ie, 330 K Kropp, J Fbbert, 153 Bonomi, Alberto, 302, 330, 365 Brigham Young University, 142 L c Lucchelli, Luigina, 302 Gag liero, Germano, 76, 86, 349 Coffee, Robert T., 117 M Cornell University,331 Corradi, Fulvia, 170 Cuitun, Louis, 318 Cuplin, Paul, 413 MaIetto, Silvana, 76, 86 Manspeaker, Joseph E., 140 Michigan State University, 212, 213, 236 Miller, John, 461 Miller, R F., 460 Ming Uan, Feng, 231 D Dameley, A.H., DVM, 251 o F Oklahoma State University, 150, 159 Ferrari, Angelo, 349 Forfa, Richard J., 393 p Formigoni, Andrea, 170 Parisini, Paoli, 170, 243 G a Guillen, Eduardo, 318 Quarantelli, Afro, 330, 365 H R Hardy, Fbnald W., 424 Herrick, John B., Fbbl, Martin G., 140, 393 Hildebran, Susan, 400 Hunt, John, 400 473 474 The Roles of Amino Acid Chelates in Animal Nutrition s Sabbiono, Alberto, 302, 330, 365 Sacchi, C., 243 Shearer, Karl D., 424 Superchi, Paola, 302, 330, 365 Suzuki, Katsuhio, 440 T Takatsuka, Takehuru, 440 u University of University of University of University of Bologna, 170, 243 Chile, 21 Ilinois, 225 Kentucky, 187, 197 University of Maryland, 140, 144, 393 University of Parma, 302, 330 University of Perugia, 191, 192 UnNersityofTurin,76,86,328 University of Washington, 424 v Volpelli, LA, 243 w Wakabayashi Takaaki, 440 Werner, Alfred, IX x Xian-Ming, Cao, 231 v Van Ping, Zhou, 231 z ZUnino, Hugo, 21 INDEX Average Daily Gain, (see Growth) Estrus, 141, 144, 146-148, 159, 165167, 243, 245-249 Fertility, 140, 153, 249 Gestation, 216 ~ 29, 421, 449 Inseminations, 183 Periglandular Rbrosis, 141, 149, 150 Pregnancy, 141, 159, 177, 182-185, 209,211,227,243,249,252-253,265, 393, 405 Reproduction/Reproductive, 170, 176, 182-185, 244, 246, 266, 393, 396 Retained Placentas, 184 Brittle Bone Disease, 349 Butterfat, (see Milk) B c Backfat, (see Carcass) Bioavailability, (see Intestinal Absorption) Biotin, 33, 416, 426 Birth Weight, 207, 213, 215, 218 Blood ~um, 352, 356, 406, 428, 432 Erythrocyte, 164 Hemoglobin, 8, 29, 30, 70, 71, 110, 162, 190,213, 231,232, 234, 235, 236, 237, 239, 449, 450, 453, 465 Hemosiderin, 223 lymphocytes, 124 Phosphorus, 352 Plasma Iron, 213 Potassium, 352 Serum, 155, 158 Sodium, 9-16, 352 Transferrin, 8, 29, 171, 212 Boron,36 Breeding ~ption (rates), 142, 146, 159, 166-167, 182, 246, 248, 262, 393, 395, 397, 398 Embryonic MortaJity, 147, 150,393 EndometriaJ Scarring, 140, 141, 149 End~s, 148, 150 Cadmium, 10-16, 26, 406 4, 9-16, 22, 24, 26-28, 32-36, 49, 67-68, 96, 154, 158, 171, 188-189, 197,200,208,293,305,331,381,424425, 433-435 ~um Amino Acid Olelate, 67-68,292, 403, 414, 417, 463 ~ydrates, 22, 47, 49, 76, 187, 197 Carcass, 20Q Backfat, 201, 259, 260-261, 266, 269270, 274, 280-282 Fat Over Rib, 201 Grade, 201 liver Copper, 405, 407 liver Iron, 214 Marbling, 201 Quality, 194-195 Cartilage, 405 Catalase, 162 Cataracts, 424, 432 Catarrhal Entrotyphlitis, 352 Cellobiose, 82-83 Cellulase, (see Fiber) Chelation, VH, 6-7, 49-51, 106, 457 Amino Acid Chelate (s), VIII, Xl, 51-59, A Absorption, (see Intestinal Absorption) Phosphatase, 353 Aluminum, 125, 141, 126, 142, 190 American Association of Feed Control Officials (MFCO), X, XI, 51 Amino Acid OleIate (see Chelation) Amino Acid Complex (see Complex) Amylase, 192 Anemia, 28-30, 223-225, 231,236,239 Arsenic, 190 Ascorbic Acid, (see Vitamin C) ATP, 3, 24, 80, 190 ~kaline ~um, 475 476 The Roles of Amino Acid Chelates in Animal Nutrition 82-83,86,93-99, 103, 106-111, 145, 149-150, 157, 159-161, 167, 171, 180-185, 191-197, 223, 251, 291, 299, 305, 311, 324, 346, 361, 370, 376, 398, 457, 462-468 133, 165201, 319, 407, Minerals CheIated to knino Acids, 86, 413 Amino Acid CheIated Mineral, 244 Diethytenetriaminepentraacetic Acid (DTPA), 303 EDTA, IX, 8, 106,303,425,433-434, 457, 458 Molar Ratio, Xl, 51 Molecular Weight, XI, 17, 51,54,70, 212, 251, 464-465 Stability Constant, 17, 55, 106,433, 458-464, 467 Choline Q-aoride, (see Vitamins) Chromium, 3, 190 Cobalt, 4,8-16,25-26,30, 100, 142, 170,190,302,305,308,335,365,368 Cobalt Amino Acid Chelate, 81,87,90, 107-108, 158, 176, 192, 197-198,245, 302,312,320,336,357,359,367,395, 404, 414, 417 Collagen, 405 Complex, Amino Acid, 108 Conception (Rates), (see Breeding) Copper, 9-16, 23-26, 29, 32, 36, 52-53, 100, 119, 126, 135, 142-143, 150, 153155,160-165,170-171,190,302,305, 308, 330, 335, 365, 368, 403-406 Copper Amino Acid Chelate, 38,40,81, 87, 90, 107-108, 132-134, 144, 158, 161-162, 165, 167, 176, 192, 197-198, 245,292,294,302,312,320,336,357, 359,367,395, 403-405, 414, 417 o D-Calcium Pantothenate, (see Vitam ins) Deficiency Copper Deficiency, 405 Iron Deficiencies, 405 Diethytenetriaminepentaacetlc Acid (DTPA), (see Chelation) Digestion,201 ~, 76, 79 ~ , 76, 79 DNA, 188 E EeIs,440, EDTA, (see Chelation) Egg~), 300, 358, 384, 372 Egg Production, 365, 380, 384 Bastin, 405 Embryonic Mortality, (see Breeding) Endometrial Scarring, (see Breeding) Endometritis, (see Breeding) Energy, 188, 247 Metabolizable Energy, 92-97, 101-102 Enteritis, 350 Epiphysitis, 400 Equine Organic Iron Supplement, 403, 405 Erysipelas, 224 Erythrocyte Superoxide Dismutase, 164, 468 Estrus, (see Breeding) Ethylenediamine tetraacetic Acid (EDTA), (see Chelation) F Farrowing, 215-216, 251-252 Fat Over Rib, (see Carcass) Fatty Acids, 274 Feed Conversion(s), 193-197, 279-281, 303, 309-310, 318, 326-327, 333, 341, 352, 373, 383, 386, 415, 421-422, 430, 443, 445, 448, 453 Feed ~, 225, 274, 413 FemoraJ Head Necrosis, 349 Fertility, (see Breeding) Fiber, 34, 49, 53 Cellulase, 192 Auorine, 22, 190 Folic Acid, (see Vitamins) G Gestation, (see Breeding) Index Growth (rates), 188, 194, 196,207,227, 232, 237-239, 279, 303, 309, 318, 340, 346, 376, 424, 443, 453 Average Daily Gain, 199 Weaning weight, 166,219 weight Gain, 193, 199, 323, 369, 375, 445 Glucose, 353 Glutathionine Peroxidase, 162 477 Iron, 8, 9-16, 24-29, 32, 36, 40, 52-53, H 59, 70, 96, 100, 126, 143, 170-171, 190, 207-212,216,222-227,231-235,246-248, 293, 302, 305, 330, 335, 365, 406 Iron Amino Acid 0leIate, 38,58,69-71, 81,87, 90, 107-108, 144, 176, 192, 197198, 207-221, 225-227, 231, 233, 239, 245, 249, 251, 266, 292, 302, 312, 320, 336, 357, 359, 367, 395, 403-404, 414, 417, 440, 463 ~on Dexban, 215, 218, 219, 224 Hatch Weight, 293 L Hematocrit, (see Blood) Hemoglobin, (see Blood) Hemosiderin, (see Blood) HstopathoIogy, 110 Hyperplasia, 187 Hypertrophy, 187 Immunity, 358, 358, 359 Immune Response, 117-118, 122, 125-126, 130, 135, 361,465 Immune System, 117 Immunoglobulin, 122-127 IgA, 123, 126 IgO, 123, 125-126 IgE, 123, 126 IgG, 123, 125-126, 129-131 19M, 123, 125-126, 129-131 V~nation, 119, 121, 122, 128 Infectious Stunting, 349 Inositol, 441 Insulin, Intestinal Absorption Absorption, 6, 21,28,47,51, 59, 171172, 184, 201, 208-209, 212, 227, 285, 293, 299, 303, 357, 361-362, 365, 377, 380-381, 407, 415, 433434, 461-466 Availability, 282, 432, 460 Bioavailability, 157, 299, 302, 324, 328, 385, 435 Iodine, 100, 158, 190, 305, 330, 335, 403 Lactase, 82, 83 ~ , 134, 179, 180, 181, 184, 185 Milk Production, 170, 178, 180, 183, 185 LO-SO, (see Toxicity) Lead, 8-16, 30, 119, 126 Upid(s), 22, 25, 33, 47, 49, 53, 187,381 Uver Copper, (see Carcass) Uver Iron, (see Carcass) Lymphocytes, (see Blood) M Magnesium, 9-16, 22-27, 34-36, 40, 5253, 80, 90, 142-154, 161-162, 189, 195, 197,212,275,305,331,380,381,424 Magnesium Amino Acid Chelate, 38, 87, 107-108, 144, 158, 161-162, 197-198, 245, ~385, 395, 403-404, 414, 417 Malabsorption Syndrome, 349 Maltase, 82-83 Manganese, 9-16,24,26-27,30,36, 6667,100, 126, 135, 142-143, 149-150, 159162, 170, 190, 197, 274, 276, 283, 285, 293,302,305,308,331,335,365,368 Manganese Amino Acid Chelate, 66-67, 81,87,90, 107-108, 132-134, 144, 158, 161-162, 176, 192, 196-198, 245, 274283, 292, 294, 302, 312, 320, 336, 357, 359, 367, 395, 403-404, 414, 417, 463 Manganese Gluconate, 278 Marbling, (see Carcass) Metabolism, 201, 227 Metabolizable Energy, (see Energy) 478 The Roles of Amino Acid Chelates in Animal Nutrition Metal Proteinate(s), lX, 51, 54 Metalloenzyme, 9, 23-24, 30, 135, 467 Milk, 173, 175, 177, 179, 181 Butterfat, 1n, 180, 181, 182 Milk Production, (see Lactation) ~urn, 15, 24, 26, 32, 36, 159160, 190,331,406 Monosaccharides, 76, 79 Morbidity, 132, 135,221-222 Mortality, 132, 135,217-221,223,227, 247-258,266, 291,293,295,298-299, 309,310,333,352,357,360,383,386, 415,421,424 Stillbirth, 246-255 Mucosal Cell, 54-58, 63, 66, 461, 462, 464 Muscle Iron, 213 Myocarditis, 352 Placental Barrier, 231 PIacentaIT~, 69, 219, 223, 232 Placental Transport, 70, 211 Plasma Iron, (see Blood) ~ , 76, 78, 189 Potassium, 9, 26, 33-36, 80, 108, 143, 161, 189, 197,223,305,331,424 Potassium Amino Acid Complex, 144, 158, 161,245, 395, ~404 Pregnancy, (see Breeding) Propionic Acid, 102 ~n, 22, 25, 47, 49, 187, 214, 244 Protein Metabolism, 88, 90, 196, 343 Protein Sparing, 88-89, 93-94, 97, 101102, 199-201, 346 Protein Synthesis, 103, 104, 188 Proteinase, 90 Purine, 214, 225 Pyridoxine, (see Vitamins) N R Niacin, (see Vitamins) Nickel, 143, 190 o Osteochondrosis lesions, 406 Osteodysgenesis, 406 Osteogenesis, 200 Osteomyelitis, 351 Osteoporosis, 349 Oxalic Acid, 5, 34, 172 Rachitis, 406 ~rus, 354, 356, 358, 358, 362 Replamin Extra Breeder Pac, 404 Reproduction, (see Breeding) Retained Placentas, (see Breeding) Rboflavin, (see Vitamins) RNA, 190, 191 Rumen Bypass, 145, 171, 463 Runt Pigs, 216, s p Saccharase, 82, 83 Pale Bird Syndrome, 349 Pantothenic Acid, (see Vitamins) Pastern, 403, 405 Pathology, 72 Periglandular Fibrosis, (see Breeding) Peroxidoxine, (see Vitamins) Phosphorus, 3, 4, 22, 24-26, 34, 36, 142, 153, 188-189, 197,200,209,330, 365,381,403,424-425,428,434 Phosphorus Amino Acid Complex, 403 Phytic Acid, 5, 27,34, 171-172, 432433, 435 Placenta, 236, 465 Selenium, 24, 154, 158, 161, 191 Silicon, 22 SOD Copper Superoxide Dismutase, 162165 Zinc Superoxide Dismutase, 162-165 Sodium, 9-16, 26, 35, 80, 142, 189, 305, 424 Soil Copper, 406 Spleen Iron, 213 Stability Constant, (see Chelation) Stillbirth, (see Mortality) Strontium, 190 479 Index Sulfur, 22, 32, 36, 142, 189, 197, 406 Superoxide Dismutase, 164 Vitamin C, (see Vitamin, Ascorbic Acid) Vitamin 0, 32, 96, 160-161, 171, 335, T Vitamin 03, (see Vitamin, Niacin) Vitamin E, 99-100, 142, 158, 160-161, 355, 356, 381 Tendon Contracture, 400 Tenosynovitis, 354 Teratogenic Bfects, (see Toxicity) Thiamine, (see Vitamins) Thyro~n, 223, 283, 284 Tin, 190 To~, 71, 145,406,413,415,468 Copper Toxicity, 405 LD-SO Studies, 72 Teratogenic Bfects, 107, 111 Transferrin, (see Blood) Trehalase, 82-83 v 245,321,355,368,403,416,441 Vitamin K, 96, 99, 245, 321, 368, 441 w Weaning Weights, (see Growth Rates) weight, 208, 333, 341, 352, 443 z Zinc, 8-16, 26-27, 30, 34, 36, 52-53, 6065, 100, 119, 126, 133, 135, 143, 150, 154, 158-162, 191, 197, 222, 235, 302, 305, 308,331, 335, 368, 406, 424, 427- 428,431-435 Vaccination, (see Immunity) Vanadium, 23, 24, 191 Vitamins, 22, 47, 187 Ascorbic Acid, 32, 142,416,426,441 Choline Chloride, 96, 308, 321, 335, 355, 368, 403, 416 D-Calcium Pantothenate, 416, 426 Folic Acid, 33, 335, 368, 403, 426, 441 Niacin, 32, 99-100, 158, 244-245, 308, 321,355,368,403,416,426 Pantothenic Acid, 33, 96, 244, 308, 321,335,355,368,403,441 Peroxidoxine, 308 Pyridoxine, 33, 96, 99, 308, 335, 368, 416, 426, 441 Riboflavin, 33, 96, 99, 244, 308, 321, 335, 355, 368, 403, 416, 426, 441 Thiamine, 33, 96, 99, 188, 308, 335, 403, 416, 426, 441 Vrtamin A, 96, 99-100, 142, 158, 160161, 245-246, 308, 321, 335, 355, 368,416,441 Vitamin 81, (see Vitamin, Thiamine) Vrtamin B2, (see Vitamin, Riboflavin) Vrtamin 86, (see Vitamin, Pyridoxine) Vitamin 812, 4, 33, 96, 99, 188, 190, 321,335,368,403,416,426,441 Zinc Amino Acid Chelate, 38, 40, 60-65, 81, 87, 90, 107-108, 132-134, 144, 158, 161-162, 176, 197-198, 245, 274, 294, 302, 312, 320, 336, 357, 359, 367, 395, 404, 414, 417, 425-427, 431-435, 463 .. .THE ROLES OF AMINO ACID CHELATES IN ANIMAL NUTRITION THE ROLES OF AMINO ACID CHELATES IN ANIMAL NUTRITION Edited by H DeWayne Ashmead Albion Laboratories, Inc Clearfield, Utah Reprint Edition... point in time these amino acids were called "metal proteinates" instead of chelates Concurrently, with the development of the amino acid chelates, a second school of thought approached animal nutrition. .. EFFICIENCY OF AMINO ACID CHELATES 86 Silvano Maletto and Germano Cagliero AN ASSESSMENT OF LONG TERM FEEDING OF AMINO ACID CHELATES 106 Robert B Jeppsen SECTION CATTLE THE USE OF AMINO ACID CHELATES