Hydrolysis of fibrinogen Paris I by plasmin

Abstract

Fibrinogen Paris I structure is characterized by the presence of elongated mutant γ chains termed γParis I (mol. wt. 52,500) which replace a large proportion of the normal γ chain population. The degradative sequence of plasmic attack on the Paris I fibrinogen molecule has been studied by dodecyl sulfate polyacrylamide gel electrophoresis of digest samples before and after disulfide bridge reduction. Two core remnant chains unique to the Paris I digest have been found and termed p1 (mol. wt. 45,500) and p2 (mol. wt. 29,900), respectively. Remnant p1 appears transiently during stage 2 digestion and probably evolves from γ Paris I chains. Further attack on p1 results in remnants which migrate in a position (designated /γ1, /β4) occupied simultaneously by derivatives of normal γ and Bβ chains. Remnant p2, whose precursor cannot be deduced with certainty, is evolved during intermediate phases of stage 3 digestion from chains (mol. wt. - 42,000) migrating in the /γ1, /β4 position; it disappears at more advanced phases of stage 3 digestion. The presence of p2 in digest samples is correlated with that of a unique form of Fragment D termed D Paris I.