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We find that, in addition to a normal fibrinopeptide A (FPA), fibrinogen Long Beach releases an abnormal FPA whose HPLC behavior suggests and whose amino acid analysis confirms the substitution of His for Arg at position 16, the thrombin cleavage site. However, this dysfibrinogen displays properties strikingly different from those previously reported to be associated with Aa 16 Arg → His substitutions. These properties include a limited release of normal FPA (18-20%) by both thrombin and batroxobin, an essentially full release of abnormal FPA (40-50%) by thrombin (1.5 NIH u/ml) in contrast to a 7-8% release of abnormal FPA by batroxobin, and a complete failure of highly purified batroxobin to clot the dysfibrinogen while generating a fragment which migrates between the B8 and y chains on SDS gel electrophoresis. The basis for these differing properties is not yet clear.

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