Clot lysis of variant recombinant fibrinogens confirms that fiber diameter is a major determinant of lysis rate

Annals of the New York Academy of Sciences

Volumn 936, Issue , 2001, Pages 331-334

  Mullin, Jennifer L ^a   Norfolk, Susan E ^a   Weisel, John W ^b   Lord, Susan T ^a,c  

^a University of North Carolina at Chapel Hill   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

^c UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

Author keywords

Fiber diameter; Lysis; Recombinant fibrinogen

Indexed keywords

FIBRINOGEN; RECOMBINANT PROTEIN; THROMBIN;

AMINO TERMINAL SEQUENCE; BLOOD CLOT LYSIS; CONFERENCE PAPER; POLYMERIZATION; PROTEIN DOMAIN; PROTEIN VARIANT; SCANNING ELECTRON MICROSCOPY; TEMPERATURE;

EID: 0034977041     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2001.tb03519.x     Document Type: Conference Paper

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11. Nonenzymatic glycosylation reduces the susceptibility of fibrin to degradation by plasmin
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13. Decreased lateral aggregation of a variant recombinant fibrinogen provides insight into polymerization mechanism
14. Characterization of purified recombinant fibrinogen: Partial phosphorylation of fibrinopeptide A
15. Strategy for recombinant multichain protein synthesis: Fibrinogen B beta-chain variants as thrombin substrates