Sea urchin fibrillar collagen 2α chain participates in heterotrimeric molecules of (1α)22α stoichiometry

In sea urchin, two fibrillar collagen chains (1 alpha and 2 alpha) have been characterized by molecular biology while two biochemically detected chains (alpha1 and alpha2) have been reported. Here, to determine the relationship between these results, Western-blotting and Edman degradation sequencing of the amino-termini of pepsinized sea urchin fibrillar collagen chains were performed. The data demonstrate that the 2 alpha chain corresponds to the alpha2 chain and is involved in the formation of heterotrimeric molecules [(1 alpha)(2)2 alpha]. (C) 2000 Elsevier Science B.V./International Society of Matrix Biology. All rights reserved.