Complete sequence of the lamprey fibrinogen .alpha. chain

Abstract

The complete amino acid sequence of the lamprey fibrinogen .alpha. chain has been determined by a combination of peptide sequencing and cDNA and genomic cloning. The chain, which has an apparent molecular weight by dodecyl sulfate-polyacrylamide gel electrophoresis of ca. 100000, is composed of 961 amino acid residues and has a calculated molecular weight of 96722. It is distinguished by a large number of 18-residue repeats in a region where mammalian fibrinogens have 13-residue repeats. The data are in accord with our previous finding that the lamprey .alpha. chain has a distinctive amino acid composition, almost half the residues being glycine, serine, or threonine. The chain differs from mammalian .alpha. chains in that there are no cysteines in the carboxy-terminal half, and thus no intrachain loop, nor are there any RGD sequences in the lamprey .alpha. chain. Taken together with previous data on the sequences of the .beta. and .gamma. chains, the findings bear significantly on our understanding of fibrin formation. The .alpha. chain also provides an interesting case of structural convergence during evolution.