Electron microscopy of fibrin Paris I

摘要: Fibrinogen Paris I, a congenital fibrinogen abnormality, is characterized by delayed fibrin aggregation and poor clot retraction owing to the replacement of normal gamma-chains mutant gamma-chains, which are termed gamma-Paris I. Available evidence indicates that structural abnormality involves amino acid sequence near COOH- terminus chain probably includes region containing gamma-chain crosslinking site. Electron microscopy was carried out on I fibrin. In place normally interwoven network branching cross-striated fibers, negatively or positively contrasted nonfibrous clumps material connected distince fibrous strands tending be thinner more irregular in width than Most fibers tended aperiodic, although cross-striations were observed occasionally specimens rarely specimens. addition, frequently showed relatively short, abruptly terminating fibers. The gross ultrastructural differences between suggest for assembly take normally, region(s) molecule possibly overlapping COOH-terminal gamma- site must preserved at least not sterically hindered.