Partial characterization of type X collagen from bovine growth‐plate cartilage Evidence that type X collagen is processed in vivo

Abstract

Sequential extraction of bovine growth-plate cartilage with 4 M guanidinium chloride and pepsin was used to identify the intact and pepsinized forms respectively of type X collagen. This collagen occurs predominantly as the processed [α₁(X)]₃ form in vivo, although the procollagen [proα₁(X)]₃ form can also be detected. The bovine proα₁ (X) and α₁(X) chains have M _r, values identical to the corresponding chick species (M _r 59 000 and 49 000). However, the pepsinized α₁(X)_p chains (M _r 47 000) are larger than those of the chick (M _r 45 000), and the bovine collagen type X is further distinguished by being disulphide-bonded within the triple-helical domain.