fibrinopeptide

On the fibrinogen α and β chains, there is a small peptide sequence (called a fibrinopeptide).

Cerastocytin contains a hydrophobic domain that binds fibrinopeptide A and in the 3-D confirmation looks very similar to the analogous region of alpha-thrombin.

Reptilase also differs from thrombin by releasing fibrinopeptide A, but not fibrinopeptide B, in its cleavage of fibrinogen.

Sulfation was first discovered by Bettelheim in bovine fibrinopeptide B in 1954 and later found be present in animals and plants but not in prokaryotes or in yeast.

Detroit is a major defect, there is fibrinopeptide release, the thrombin time is prolonged, there is an inhibitory effect on normal clotting and there is abnormal bleeding.