Bovine collagen. II. Electrophoresis of collagen fractions

Abstract

Summary. Vertical starch gel electrophoresis was used to separate components of neutral salt soluble (NSS) and acid soluble (AS) collagens, and of eucollagens, from muscle, skin and tendon of bovines of different age. The relative proportions of the separated components were assessed spectrophotometrically.The electrophoretograms indicated that the greater difficulties of extraction which distinguish AS from NSS collagen reflect a greater measure of cross‐bonding between the α chains of the former.They also indicated that there was a marked increase in the proportion of components having intramolecular cross bonds, in both NSS and AS collagens and in the three tissues studied, between the 5th and 9th month of gestation. In older animals there were also indications of an enhanced degree of intermolecular cross bonding.Such changes help explain the increased toughness of the meat from older bovines despite a lower percentage of collagen.