1Leterme, P (2002) Recommendations by health organizations for pulse consumption. Br J Nutr 88, Suppl. 3, S239–S242.
2Marquez, UM & Lajolo, FM (1990) Nutritional value of cooked beans Phaseolus vulgaris and their isolated major protein fractions. J Sci Food Agric 53, 235–242.
3Gepts, P & Bliss, F (1994) Enhanced available methionine associated with higher phaseolin levels in common bean seeds. Theor Appl Genet 69, 47–53.
4Deshpande, SS & Damodaran, S (1989) Structure-digestibility relationship of legume 7S proteins. J Food Sci 54, 108–113.
5Jivotovskaya, A, Senyuk, V, Rotari, V, Horstmann, C & Vaintraub, I (1996) Proteolysis of phaseolin in relation to its structure. J Agric Food Chem 44, 3768–3772.
6Deshpande, SS & Nielsen, SS (1987) In vitro enzymatic hydrolysis of phaseolin, the major storage protein of Phaseolus vulgaris L. J Food Sci 52, 1326–1329.
7Montoya, CA, Lallès, JP, Beebe, S, Montagne, L, Souffrant, WB & Leterme, P (2006) Influence of the Phaseolus vulgaris phaseolin level of incorporation, type and thermal treatment on gut characteristics in rats. Br J Nutr 95, 116–123.
8Koening, RL, Singh, SP & Gepts, P (1990) Novel phaseolin types in wild and cultivated common bean (Phaseolus vulgaris, Fabaceae). Econ Bot 44, 50–60.
9Kami, J & Gepts, P (1994) Phaseolin nucleotide sequence diversity in Phaseolus vulgaris. Genome 37, 751–757.
10Montoya, CA, Lallès, JP, Beebe, S, Souffrant, WB & Leterme, P (2005) Effect of the types of Phaseolus vulgaris phaseolin and thermal treatment on in vitro sequential hydrolysis by pepsin and pancreatin. In Proceedings of the Fouth International Food Legumes Research Conference, pp. 61–62 [Kharkwal, MC, editor]. New Delhi: Indian Society of Genetics and Plant Breeding.
11Fukuda, T, Maruyama, N, Kanazawa, A, Abe, A, Shimamoto, Y, Hiemori, M, Tsuji, H, Tanisaka, T & Utsumi, S (2005) Molecular analysis and physico-chemical properties of electrophoretic variants of wild soybean Glycine soja storage proteins. J Agric Food Chem 53, 3658–3665.
12Begbie, R & Ross, AW (1993) Resistance of the kidney bean reserve protein, phaseolin, to proteolysis in the porcine digestive tract. J Sci Food Agric 61, 301–307.
13Santoro, LG, Grant, G & Pusztai, A (1999) In vivo degradation and stimulating effect of phaseolin on nitrogen secretion in rats. Plant Foods Hum Nutr 53, 223–236.
14Le Gall, M, Quillien, L, Guéguen, J, Rogniaux, H & Sève, B (2005) Identification of dietary and endogenous ileal protein losses in pigs by immunoblotting and mass spectrometry. J Nutr 135, 1215–1222.
15Salgado, P, Montagne, L, Freire, JPB, Ferreira, R, Teixeira, A, Bento, O, Abreu, M, Toullec, R & Lallès, JP (2002) Legume grains enhance ileal losses of specific endogenous serine-protease proteins in weaned pigs. J Nutr 132, 1913–1920.
16Mrad de Osorio, A & Cardozo de Martinez, C (1999) Principios basicos para el manejo de animales de laboratorio. (Basic Principles for the Handling of Laboratory Animals). Bogota: Universidad Nacional de Colombia.
17Lowry, OH, Rosebrough, NJ, Farr, AL & Randall, RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193, 265–275.
18Boulard, CH & Lecroisey, A (1982) Specific antisera produced by direct immunization with slices of polyacrylamide gel containing small amounts of protein. J Immunol Methods 50, 221–226.
19Shevchenko, A, Wilm, M, Vorm, O & Mann, M (1996) Mass spectrometry sequencing of proteins from silver-stained polyacrylamide gels. Anal Chem 68, 850–858.
20Wattenberg, A, Organ, AJ, Schneider, K, Tyldesley, R, Bordoli, R & Bateman, RH (2002) Sequence dependent fragmentation of peptides generated by MALDI quadrupole time-of-flight (MALDI Q-TOF) mass spectrometry and its implications for protein identification. J Am Soc Mass Spectr 13, 772–783.
21Pappin, DJC, Hojrup, P & Bleasby, AJ (1993) Rapid identification of proteins by peptide-mass fingerprinting. Curr Biol 3, 327–332.
22Duncan, DB (1955) Multiple range and multiple F-tests. Biometrics 11, 1–42.
23Hall, TC, McLeester, RC & Bliss, FA (1977) Equal expression of the maternal and paternal alleles for polypeptide subunits of the major storage protein of the bean Phaseolus vulgaris L. Plant Physiol 59, 1122–1124.
24Slightom, JL, Drong, RF, Klassy, RC & Hoffman, LM (1985) Nucleotide sequence from phaseolin cDNA clones: the major storage proteins from Phaseolus vulgaris are encoded by two unique gene families. Nucleic Acids Res 13, 6483–6498.
25Alli, I, Gibbs, BF, Okoniewska, MK, Konishi, Y & Dumas, F (1993) Identification and characterization of phaseolin polypeptides in a crystalline protein isolated from white kidney beans (Phaseolus vulgaris). J Agric Food Chem 41, 1830–1834.
26Kami, J, Becerra, V, Debouck, DG & Gepts, P (1995) Identification of presumed ancestral DNA sequences of phaseolin in Phaseolus vulgaris. Proc Natl Acad Sci USA 92, 1101–1104.
27Banerjee, R, Das, K, Ravishankar, R, Suguna, K, Surolia, A & Vijayan, M (1996) Conformation, protein–carbohydrate interactions and a novel subunit association in the refined structure of peanut lectin-lactosa complex. J Mol Biol 259, 281–296.
28Bollini, R & Vitale, A (1981) Genetic variability in charge microheterogeneity and polypeptide composition of phaseolin, the major storage protein of Phaseolus vulgaris; and peptide maps of its three major subunits. Physiol Plant 52, 96–100.
29Hodgkinson, SM, Souffrant, WB & Moughan, PJ (2003) Comparison of the enzyme-hydrolyzed casein, guanidination, and isotope dilution methods for determining ileal endogenous protein flow in the growing rat and pig. J Anim Sci 81, 2525–2534.
30Hara, H, Nishi, T & Kasai, TA (1995) Protein less sensitive to trypsin, guanidinated casein, is a potent stimulator of exocrine pancreas in rats. Proc Soc Exp Biol Med 210, 278–284.
31Savoie, L (1994) Digestion and absorption of food: usefulness and limitations of in vitro models. Can J Physiol Pharmacol 72, 407–414.
32Savoie, L, Agudelo, RA, Gauthier, SF, Marin, J & Pouliot, Y (2005) In vitro determination of the release kinetics of peptides and free amino acids during the digestion of food proteins. J AOAC Int 88, 935–948.