THE STRUCTURES OF FIBRINOGEN AND FIBRIN

Abstract

In recent years, a major effort has been under way in several laboratories to determine the primary structure of the three nonidentical chains of human fibrinogen. The bulk of these efforts have been centered in three laboratories—Blomback's in Stockholm, Henschen's in Munich, and the one in La Jolla. All three groups have published numerous reports dealing with various portions of the structure. The most significant feature to emerge from the primary structure studies on fibrinogen so far has been the homology observed among the three nonidentical chains. Clearly, all three chains have descended from a common ancestor. This chapter describes the way such an evolutionary perspective is consistent with certain three-dimensional structures proposed for fibrinogen and is inconsistent with others. The human fibrinogen molecule contains 29–31 disulfide bridges, the ambiguity residing in the α-chains, which contain either 8 or 10 cysteine residues; β -chains and γ -chains have 11 and 10 cysteine, respectively.