Type I collagen synthesis by rats fed beans (Phaseolus vulgaris, L.) as the protein source.
Type I collagen synthesis was studied in 12 female Wistar rats weighing 60 +/- 5 g at the beginning of the experiment. The animals were fasted for 24 h and then injected ip with 10 microCi uniformly labeled [14C]-glycine. Two hours later, groups of 4 animals each were fed balanced diets (10.7 +/- 0.4% protein) containing raw beans (Phaseolus vulgaris, L.), cooked beans or casein (control) as the single protein source, ad libitum. The animals were killed after 4 days and collagen was extracted from the tail and calcaneal tendons. Food intake and weight gain of rats fed raw beans (22 g, 0 g) were considerably less than rats fed cooked beans (38 g, 9 g) and casein (44 g, 22 g). Collagen was quantitated on the basis of hydroxyproline and corresponded to 0.1, 0.2 and 0.2% rat body weight, with specific radioactivity of 1.2, 1.6 and 4.2 microCi/g, for the rats fed raw beans, cooked beans and casein, respectively. The results indicate that rats fed either bean protein synthesized less collagen than those fed casein (P < 0.05). Although the food intake and extractable collagen of rats fed cooked beans were similar to those of casein-fed rats, weight gain and collagen specific radioactivity were less.
Oliveira
A C
AC
Departamento de Planejamento Alimentar e Nutrição, Faculdade de Engenharia de Alimentos, Universidade Estadual de Campinas, SP, Brasil.
Vidal
B C
BC
D000818:Animals; D002250:Carbon Radioisotopes; D002364:Caseins / Q000008:administration & dosage; D003094:Collagen / Q000032:analysis / Q000096:biosynthesis*; D003296:Cooking; D004044:Dietary Proteins / Q000008:administration & dosage*; D007887:Fabaceae; D005260:Female; D010946:Plants, Medicinal; D051381:Rats; D017208:Rats, Wistar; D013623:Tail / Q000737:chemistry; D013710:Tendons / Q000737:chemistry
D002250:Carbon Radioisotopes; D002364:Caseins; D004044:Dietary Proteins; D003094:Collagen