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109. Rodriguez-Estrada, M.T., Penazzi, G., Caboni, M.F., Bertacco, G., Lercker, G. (1997). Effect of different cooking methods on some lipid and protein components of hamburgers. Meat Sci., 45, 365 375. 110. Piva, G., Moschini, M., Fiorentini, L., Masoero, F. (2001). Effect of temperature, pressure and alkaline treatments on meat meal quality. Anim. Feed Sci. Tech., 89, 59 68. 111. Cor eld, M.C., Wood, C., Robson, A., Williams, M.J., Woodhouse, J.M. (1967). The formation of lysinoalanine during the treatment of wool with alkali. Biochem. J., 103, 15C 16C. 112. Friedman, M., Whit eld, R.E., Tillin, S. (1973). Enhancement of the natural ame resistance of wool. Text. Res. J., 43, 212 217. 113. Friedman, M., Noma, A.T. (1970). Cystine content of wool. Text. Res. J., 40, 1073 1078. 114. Friedman, M., Orraca-Tetteh, R. (1978). Hair as an index of protein malnutrition, in Nutritional Improvement of Food and Feed Proteins (ed. M. Friedman), Plenum Press, New York, pp. 131 154. 115. Zahn, H., Gattner, H.G. (1997). Hair sulfur amino acid analysis. Exp. Suppl., 78, 239 258. 116. Han, Y., Parsons, C.M. (1991). Protein and amino acid quality of feather meal. Poult. Sci., 70, 812 822. 117. Touloupis, C., Vassiliadis, A. (1977). Lysinoalanine formation in wool after treatments with some phosphate salts. Adv. Exp. Med. Biol., 86 B, 187 195. 118. Shinbo, H. (1998). An enzyme that catalyzes the synthesis of lanthionine in the silkworm, Bombyx mori. Comp. Biochem. Physiol., 91, 301 308. 119. Shetty, J.K., Kinsella, J.E. (1980). Lysinoalanine formation in yeast proteins isolated by alkaline methods. J. Agric. Food Chem., 28, 798 800. 120. Chung, S.-Y., Swaisgood, H.E., Catignani, G.L. (1986). Effects of alkali treatment and heat treatment in the presence of fructose on digestibility of food proteins as determined by an immobilized digestive enzyme assay (IDEA). J. Agric. Food Chem., 34, 579 584. 121. De Groot, A.P., Slump, P., Feron, V.J., Van Beek, L. (1976). Effects of alkali treated proteins: feeding studies with free and protein bound lysinoalanine in rats and other animals. J. Nutr., 106, 1527 1538. 122. Slump, P. (1978). Lysinoalanine in alkali-treated proteins and factors in uencing its biological activity. Ann. Nutr. Aliment., 32, 271 279. 123. Savoie, L., Parent, G., Galibois, I. (1991). Effects of alkali treatment on the in-vitro digestibility of proteins and the release of amino acids. J. Sci. Food Agric., 56, 363 372. 124. Savoie, L. (1984). Effect of protein treatment on the enzymatic hydrolysis of lysinoalanine and other amino acids. Adv. Exp. Med. Biol., 177, 413 422. 125. Swaisgood, H.E., Catignani, G.L. (1985). Digestibility of modi ed milk proteins: nutritional implications. J. Dairy Sci., 68, 2782 2790. 126. Possompes, B., Berger, J. (1986). Effect of severely alkali-treated casein on gastrointestinal transit and selected intestinal enzyme activities. Adv. Exp. Med. Biol., 199, 517 530. 127. Friedman, M., Gumbmann, M.R., Savoie, L. (1982). The nutritional value of lysinoalanine as a source of lysine for mice. Nutr. Rep. Int., 26, 937 943.
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DIETARY SIGNIFICANCE OF PROCESSING-INDUCED LYSINOALANINE
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128. Nishino, N., Masaki, Y., Uchida, S. (1996). Changes in nitrogenous compounds and rates of in situ N loss of soybean meal treated with sodium hydroxide or heat. J. Agric. Food Chem., 44, 2667 2671. 129. Nishino, N., Uchida, S., Ohshima, M. (1995). Formation of lysinoalanine following alkaline processing of soya bean meal in relation to the degradability of protein in the rumen. J. Sci. Food Agric., 68, 59 64. 130. Hayashi, R. (1982). Lysinoalanine as a metal chelator. An implication for toxicity. J. Biol. Chem., 257, 13896 13898. 131. Friedman, M., Grosjean, O.-K., Zahnley, J.C. (1985). Carboxypeptidase inhibition by alkali-treated food proteins. J. Agric. Food Chem., 33, 208 213. 132. Friedman, M., Grosjean, O.-K.K., Zahnley, J.C. (1985). Metalloenzyme inhibition by lysinoalanine, phenylethylaminoalanine, and alkali-treated food proteins. Fed. Proc., 44, 6351. 133. Friedman, M., Grosjean, O.K., Zahnley, J.C. (1986). Inactivation of metalloenzymes by food constituents. Food Chem. Toxicol., 24, 897 902. 134. Friedman, M., Grosjean, O.K., Zahnley, J.C. (1986). Inactivation of metalloenzymes by lysinoalanine, phenylethylaminoalanine, alkali-treated food proteins, and sulfur amino acids. Adv. Exp. Med. Biol., 199, 531 560. 135. Possompes, B., Berger, J. (1991). Effect of severely alkali treated casein on gastrointestinal transit and selected intestinal enzyme activities, in Nutritional and Toxicological Consequences of Food Processing (ed. M. Friedman), Plenum, New York, pp. 517 530. 136. Friedman, M., Finot, P.A. (1991). Improvement in the nutritional quality of bread. Adv. Exp. Med. Biol., 289, 415 445. 137. Friedman, M. (1996). Food browning and its prevention: an overview. J. Agric. Food Chem., 44, 631 653. 138. Sternberg, M., Kim, C.Y. (1979). Growth response of mice and Tetrahymena pyriformis to lysinoalanine-supplemented wheat gluten. J. Agric. Food Chem., 27, 1130 1132. 139. Robbins, K.R., Baker, D.H., Finley, J.W. (1980). Studies on the utilization of lysinoalanine and lanthionine. J. Nutr., 110, 907 915. 140. Finot, P.A., Bujard, E., Arnaud, M. (1977). Metabolic transit of lysinoalanine (LAL) bound to protein and of free radioactive 14C]-lysinoalanine. Adv. Exp. Med. Biol., 86 B, 51 71. 141. Struthers, B.J., Dahlgren, R.R., Hopkins, D.T. (1977). Biological effects of feeding graded levels of alkali treated soybean protein containing lysinoalanine (N( ) 2 carboxyethyl] L lysine) in Sprague Dawley and Wistar rats. J. Nutr., 107, 1190 1199. 142. Struthers, B.J., Brielmaier, J.R., Raymond, M.L. (1980). Excretion and tissue distribution of radioactive lysinoalanine, N -DL-(2-amino-2-carboxyethyl)-U-14C-llysine (LAL) in Sprague-Dawley rats. J. Nutr., 110, 2065 2077. 143. Kawamura, Y., Hayashi, R. (1988). Lysinoalanine degrading enzymes of various animal kidneys. Agric. Biol. Chem., 51, 2289 2290. 144. Gould, D.H., MacGregor, J.T. (1977). Biological effects of alkali-treated protein and lysinoalanine: an overview. Adv. Exp. Med. Biol., 86 B, 29 48.
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