Free Access
Reprod. Nutr. Dev.
Volume 41, Number 3, May-June 2001
Page(s) 227 - 238


Adibi S.A., Mercer D.W., Protein digestion in human intestine as reflected in luminal, mucosal and plasma amino acids concentrations after meals, J. Clin. Invest. 52 (1973) 1586-1594.
Allen L.H., Calcium bioavailability and absorption: a review, Am. J. Clin. Nutr. 35 (1982) 783-808.
Anderson J.J.B., Nutritional biochemistry of calcium and phosphorus, J. Nutr. Biochem. 2 (1991) 300-307.
Anfinsen C.B., Scheraga, H.A., Experimental and theoretical aspects of protein folding, Adv. Protein Chem. 29 (1975) 205-299.
Berliner L.J., Koga K., a-lactalbumin binding to membranes: evidences for a partially buried protein, Biochem. 26 (1987) 3006-3009.
Berliner L.J., Ellis P.D., Murakami K., Manganese (II) electron spin resonance and Cadmiun-113 nuclear magnetic resonance evidence for the nature of calcium binding site in a-lactalbumins, Biochem. 22 (1983) 5063-5068.
Berliner L.J., Meinholtz D.C., Hirai Y., Musci G., Thompson M.P., Functional implications resulting from disruption of the calcium-binding loop in bovine $\alpha$-lactalbumin, J. Dairy Sci. 74 (1991) 2394-2402.
Cheftel J.-C., Cuq J.-L., Lorient D., Protéines alimentaires, Lavoisier. Tech & Doc, Paris, 1985, pp. 156-192.
Church F.C., Swaisgood H.E., Porter D.H., Catignani G.L., Spectrophotometric assay using Ophthaldialdehyde for determination of proteolysis in milk and isolated milk proteins, J. Dairy Sci. 66 (1983) 1219-1227.
Cook G.C., Impairment of glycine absorption by glucose and galactose in man, J. Physiol. 218 (1971) 61-71.
Cramer C.F., Copp D.H., Progress and rate of absorption of radiostrontium through intestinal tracts of rats, Proc. Soc. Exp. Biol. Med. 102 (1959) 514-517.
Dent C.E., Schilling J.A., Studies on the absorption of proteins: the amino acid pattern in the portal blood, Biochem. J. 44 (1949) 318-332.
de Wit J.N., Klarenbeek G., Effect of various heat treatments on structure and solubility of whey proteins, J. Dairy Sci. 67 (1984) 2701-2710.
Fersht A., Enzymes: structure and mechanism, Freedman and Co., San Francisco, 1977.
Fiske C.H., Subbarow U., The colorimetric determination of phosphorus, J. Biol. Chem. 66 (1925) 375-400.
Freund R.J., Littel R.C., Spector P.C., SAS system for linear models, SAS Institute Inc., Cary, NC, USA, 1986.
Fushiki T., Yamamoto N., Naeshiro I., Iwai K., Digestion of $\alpha$-lactalbumin in the rat gastrointestinal tracts, Agric. Biol. Chem. 50 (1986) 95-100.
Galibois I., Nunes C.S., Rerat A., Savoie L., Net appearance of amino acids in portal blood during the digestion of casein or rapseed proteins in the pig, Can. J. Physiol. Pharmacol. 67 (1989) 1409-1417.
Hagemeister H., Antila P., Oro-ileal digestibility of homoarginine-labelled $\beta$-lactoglobulin and casein in adult miniature pigs, J. Anim. Physiol. Anim. Nutr. 72 (1994) 86-91.
Hall T.C., Lehmann H., Experiments on the practicability of increasing calcium absorption with protein derivatives, Biochem. 38 (1944) 117-119.
Kronman M.J., Characteristics of the binding of Ca2+ and other divalent metal ions to bovine a-lactalbumin, J. Biol. Chem. 25 (1981) 8582-8587.
Lee Y.S., Noguchi T., Naito H., An enhanced intestinal absorption of calcium in the rat directly attributed to dietary casein, Agric. Biol. Chem. 43 (1979) 2009-2011.
Lee Y.S., Noguchi T., Naito H., Phosphopeptides and soluble calcium in small intestine of rats given a casein diet, Br. J. Nutr. 43 (1980) 457-467.
Lieske B., Konrad G., Interrelation between pH and availability of $\alpha$-lactalbumin and $\beta$-lactoglobulin for proteolysis by papain, Int. Dairy J. 6 (1996) 359-370.
MacLeod A., Fedio W.M., Chu L., Ozimek L., Binding of retinoic acid of $\beta$-lactoglobulin variants A and B: Effect of peptic and tryptic digestion on the protein-ligand complex, Milchwissenschaft. 51 (1996) 3-7.
Marcus C.S., Lengemann F.W., Absorption of Ca45 and Sr85 from solid and liquid food at various levels of the alimentary tract of rat, J. Nutr. 77 (1962) 155-160.
Matthews D.M., Adibi S.A., Peptide absorption, Gastroenterology 71 (1976) 151-161.
Pantako T.O., Passos M., Desrosiers T., Amiot J., Effet des protéines laitières sur l'absorption de Ca et P mesurée par les variations temporelles de leurs teneurs dans l'aorte et la veine porte chez le rat, Int. Dairy J. 4 (1994) 37-38.
Papiz M.Z., Sawyer L., Eliopoulos E.E., North A.C.T., Findlay J.B.C., Sivaprasadarao R., Jones J., Newcomer M.E., Kraulis P.J., The structure of $\beta$-lactoglobulin and its similarity to plasma retinol-binding protein, Nature 324 (1986) 383-385.
Patocka G., Jelen P., Calcium association with isolated whey proteins, Can. Inst. Food Sci. Technol. J. 24 (1991) 218-223.
Puyol P., Perez M.D., Ena M.J., Calvo M., Effect of retinol and fatty acid binding by bovine b-lactoglobulin on its resistance to trypsin digestion, Int. Dairy J. 3 (1993) 589-597.
Raven A.M., Lengemann F.W., Wasserman R.H., Studies of the effect of lysine on the absorption of radiocalcium and radiostrontium by the rat, J. Nutr. 72 (1960) 29-36.
Reddy M.I., Navin K.D.K., Kinsella J.E., Structural and conformational basis of the resistance of $\beta$-lactoglobulin to peptic and chymotryptic digestion, J. Agric. Food Chem. 36 (1988) 737-741.
Reiser S., Christiansen P.A., Intestinal transport of amino acids as affectd by sugars, Am. J. Physiol. 216 (1969) 915-924.
Sato R., Noguchi T., Naito H., The necessity for the phosphate portion of casein molecules to enhance Ca absorption from the small intestine, Agric. Biol. Chem. 47 (1983) 2145-2147.
Sato R., Noguchi T., Naito H., Casein phosphopeptides (CPP) enhance calcium absorption from the small ligated Segment of rats small intestine, J. Nutr. Sci. Vitaminol. 49 (1986) 2009-2011.
Scanff P., Savalle B., Miranda G., Pélissier J.-P., Guilloteau P., Toullec R., In vivo digestion of milk proteins. Effect of technological treatments, J. Agric. Food Chem. 38 (1990) 1623-1630.
Schaafsma G., Rolls B.A., Blakeborough P., Effects of milk versus plant proteins on bioavailability of micronutrients, Bull. of the IDF 253 (1990) 55-60.
Schimidt D.G., Poll J.K., Enzymatic hydrolysis of whey proteins. Hydrolysis of $\alpha$-lactalbumin or $\beta$-lactoglobulin in buffer solutions by proteolytic enzymes, Neth. Milk Dairy J. 45 (1991) 240-255.
Stuart D.I., Acharya K.R., Walker N.P.C., Smith S.G., Lewis M., Phillips D.C., $\alpha$-lactalbumin possesses a novel calcium binding loop, Nature 324 (6092) (1986) 84-87.
Takada Y., Aoe S., Kumegawa M., Whey protein stimulates the proliferation and the differentiation of osteoblast MC3T3-E1 cells, Biochem. Biophys. Res. commun. 223 (1996) 445-449.
Takada Y., Yahiro M., Nakajima I., Effect of milk components on calcium absorption and bone metabolism, in: Yamauchi K., Imamura T., Morita T. (eds.), Kouseikan, Tokyo, 1993, characterization of milk component and health, pp. 171-185.
Takada Y., Kobayashi N., Matsuyama H., Kato K., Yamamura J., Yahiro M., Kumegawa M., Aoe S., Whey proteins suppresses the osteoclast-mediated bone resorption and osteoclast celle formation, Int. Dairy J. 7 (1997) 821-825.
Yvon M., Pélissier J.-P., Characterization and kinetics of evacuation of peptides resulting from casein hydrolysis in the stomach of the calf, J. Agric. Food Chem. 35 (1987) 148-156.
Yvon M., Van Hille I., Pélissier J.-P., Guilloteau P., Toullec R., In vivo milk digestion in the calf abomasum. II. Milk and whey proteolysis, Reprod. Nutr. Dev. 24 (1984) 835-843.
Ziegler E.E., Formon S.J., Lactose enhances mineral absorption in infancy, J. Pediat. Gastroenterol. Nutr. 2 (1983) 288-294.
Warme P.K., Momany F.A., Rumball S.V., Tuttle R.W., Scheraga H.A., Computations of structures homologous proteins. $\alpha$-lactalbumin from lysozyme, Biochemistry 13 (1974) 768-782.
Wasserman R.H., Comar C.L., Nold M.M., The influence of amino acids and other organic compounds on the gastrointestinal absorption of calcium45 and strontium89 in the rat, J. Nutr. 58 (1956) 371-383.
Wasserman R.H., Comar C.L., Schooley J.C., Lengemann F.W., Interrelated effects of L-lysine and other dietary factors on the gastrointestinal absorption of calcium45 in the rat and chick, J. Nutr. 62 (1957) 367-376.
Webb E.C., Enzyme nomenclature, IUB MB, Academic Press, New York, 1992, 403.


Copyright INRA, EDP Sciences

Current usage metrics show cumulative count of Article Views (full-text article views including HTML views, PDF and ePub downloads, according to the available data) and Abstracts Views on Vision4Press platform.

Data correspond to usage on the plateform after 2015. The current usage metrics is available 48-96 hours after online publication and is updated daily on week days.

Initial download of the metrics may take a while.