The impaired polymerization of fibrinogen Longmont (Bβ166Arg→Cys) is not improved by removal of disulfide-linked dimers from a mixture of dimers and cysteine-linked monomers

Blood

Volumn 98, Issue 3, 2001, Pages 661-666

  Lounes, Karim C ^a,b,c,d,e   Lefkowitz, Jerry B ^a,b,c,d,e   Henschen Edman, Agnes H ^a,b,c,d   Coates, Andrew I ^a,b,c,d,e   Hantgan, Roy R ^a,b,c,d,e   Lord, Susan T ^a,b,c,d,e  

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

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

^c UNIVERSITY OF COLORADO SCHOOL OF MEDICINE   (United States)

^d UNIVERSITY OF CALIFORNIA   (United States)

^e WAKE FOREST SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ARGININE; CYSTEINE; FIBRINOGEN; FIBRINOGEN LONGMONT; FIBRINOPEPTIDE A; FIBRINOPEPTIDE B; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BLEEDING DISORDER; BLOOD CLOTTING; DIMERIZATION; DISULFIDE BOND; DYSFIBRINOGENEMIA; FEMALE; GEL FILTRATION; HUMAN; LIGHT SCATTERING; PRIORITY JOURNAL; PROTEIN POLYMERIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN SECRETION; SEQUENCE ANALYSIS; TURBIDITY;

EID: 0035437197     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.V98.3.661     Document Type: Article

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