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

• Published in: Blood Vol. 98; no. 3; pp. 661 - 666
• Main Authors: Lounes, Karim C., Lefkowitz, Jerry B., Henschen-Edman, Agnes H., Coates, Andrew I., Hantgan, Roy R., Lord, Susan T.
• Format: Journal Article
• Language: English
• Published: Washington, DC Elsevier Inc 01.08.2001; The Americain Society of Hematology
• Subjects: Adult; Amino Acid Substitution - genetics; Biological and medical sciences; Cysteine - genetics; Cysteine - metabolism; Dimerization; Disulfides; Female; Fibrin - metabolism; Fibrinogens, Abnormal - biosynthesis; Fibrinogens, Abnormal - chemistry; Fibrinogens, Abnormal - genetics; Fibrinogens, Abnormal - metabolism; Fibrinolysin - metabolism; Hematologic and hematopoietic diseases; Humans; Kinetics; Medical sciences; Molecular Weight; Platelet diseases and coagulopathies; Polymers - chemistry; Thrombin - metabolism; Human; Pathogenesis; Genetic variant; Beta-Peptide chain; Abnormal fibrinogen; Polymerization; Adult; Female; Hemopathy; Mutation; Coagulopathy; Dysfibrinogenemia

This study identified a new substitution in the Bβ chain of an abnormal fibrinogen, denoted Longmont, where the residue Arg166 was changed to Cys. The variant was discovered in a young woman with an episode of severe hemorrhage at childbirth and a subsequent mild bleeding disorder. The neo-Cys resid...