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The detailed proof of the amino acid sequence of the 140 residues (16,193 daltons) of the light chain of bovine factor X1 (Stuart factor) is presented. Sequence analyses were performed on fragments obtained after chemical cleavage of asparagine-glycine and tryptophanyl peptide bonds and after various enzymatic digestion procedures. Twelve gamma-carboxyglutamyl residues are clustered in the amino-terminal 39 residues and 13 half-cystine residues are found in the carboxyl-terminal 91 residues, suggesting two domains in the light chain, one exceptionally anionic and the other extensively cross-linked by disulfides.
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