fibrinopeptide-b and Lupus-Erythematosus--Systemic

fibrinopeptide-b has been researched along with Lupus-Erythematosus--Systemic* in 2 studies

Reviews

1 review(s) available for fibrinopeptide-b and Lupus-Erythematosus--Systemic

Article	Year
Radioimmunoassays of human fibrinopeptides A and B. Polskie Archiwum Medycyny Wewnetrznej, 1978, Volume: 59, Issue:1 Topics: Disseminated Intravascular Coagulation; Fibrinogen; Fibrinopeptide A; Fibrinopeptide B; Humans; Lupus Erythematosus, Systemic; Pulmonary Embolism; Radioimmunoassay; Thrombin; Thrombophlebitis	1978

Other Studies

1 other study(ies) available for fibrinopeptide-b and Lupus-Erythematosus--Systemic

Article	Year
Fibrinogen Matsumoto V: a variant with Aalpha19 Arg-->Gly (AGG-->GGG). Comparison between fibrin polymerization stimulated by thrombin or reptilase and fibrin monomer polymerization. Thrombosis and haemostasis, 2001, Volume: 85, Issue:1 Fibrinogen Matsumoto V (M-V) is a dysfibrinogen identified in a 52-year-old woman with systemic lupus erythematous. The triplet AGG encoding the amino acid residue Aalpha19 was replaced by GGG, resulting in the substitution of Arg-->Gly. Residue Aalpha19 has been shown to be one of the most important amino acids in the so-called 'A' site or alpha-chain knob. The thrombin-catalyzed release of fibrinopeptide A from M-V fibrinogen was only slightly delayed yet release of fibrinopeptide B was significantly delayed. Both thrombin-catalyzed fibrin polymerization and fibrin monomer polymerization were markedly impaired compared to normal fibrinogen. In addition, reptilase-catalyzed fibrin polymerization of M-V was much more impaired than thrombin-catalyzed fibrin polymerization. These results indicate 'B' and/or 'b' site of M-V fibrinogen play a more important role in thrombin-catalyzed fibrin polymerization than that of normal control fibrinogen. Topics: Batroxobin; Blood Coagulation Tests; DNA Mutational Analysis; Female; Fibrin; Fibrinogens, Abnormal; Fibrinopeptide A; Fibrinopeptide B; Genetic Variation; Humans; Kinetics; Lupus Erythematosus, Systemic; Middle Aged; Point Mutation; Thrombin	2001

Article

Year

Fibrinogen Matsumoto V: a variant with Aalpha19 Arg-->Gly (AGG-->GGG). Comparison between fibrin polymerization stimulated by thrombin or reptilase and fibrin monomer polymerization.

Thrombosis and haemostasis, 2001, Volume: 85, Issue:1

Fibrinogen Matsumoto V (M-V) is a dysfibrinogen identified in a 52-year-old woman with systemic lupus erythematous. The triplet AGG encoding the amino acid residue Aalpha19 was replaced by GGG, resulting in the substitution of Arg-->Gly. Residue Aalpha19 has been shown to be one of the most important amino acids in the so-called 'A' site or alpha-chain knob. The thrombin-catalyzed release of fibrinopeptide A from M-V fibrinogen was only slightly delayed yet release of fibrinopeptide B was significantly delayed. Both thrombin-catalyzed fibrin polymerization and fibrin monomer polymerization were markedly impaired compared to normal fibrinogen. In addition, reptilase-catalyzed fibrin polymerization of M-V was much more impaired than thrombin-catalyzed fibrin polymerization. These results indicate 'B' and/or 'b' site of M-V fibrinogen play a more important role in thrombin-catalyzed fibrin polymerization than that of normal control fibrinogen.

Topics: Batroxobin; Blood Coagulation Tests; DNA Mutational Analysis; Female; Fibrin; Fibrinogens, Abnormal; Fibrinopeptide A; Fibrinopeptide B; Genetic Variation; Humans; Kinetics; Lupus Erythematosus, Systemic; Middle Aged; Point Mutation; Thrombin

2001