Sea urchin fibrillar collagen 2alpha chain participates in heterotrimeric molecules of (1alpha)(2)2alpha stoichiometry.
In sea urchin, two fibrillar collagen chains (alpha1 and alpha2) 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 2alpha chain corresponds to the alpha2 chain and is involved in the formation of heterotrimeric molecules [(1alpha)(2)2alpha].
Cluzel
C
C
Institut de Biologie et Chimie des Protéines, CNRS, Unité Mixte de Recherche 5086, Université Claude Bernard, 7 passage du Vercors, 69367, cedex 07, Lyon, France.
Lethias
C
C
Garrone
R
R
Exposito
J Y
JY
D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western; D003094:Collagen / Q000737:chemistry* / Q000276:immunology; D010434:Pepsin A / Q000737:chemistry; D020836:Protein Structure, Quaternary; D012617:Sea Urchins / Q000737:chemistry*
D003094:Collagen; D010434:Pepsin A