fibrinopeptide


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fibrinopeptide

 [fi″brĭ-no-pep´tīd]
either of two peptides (A and B) split off from fibrinogen during blood clotting by the action of thrombin.
Miller-Keane Encyclopedia and Dictionary of Medicine, Nursing, and Allied Health, Seventh Edition. © 2003 by Saunders, an imprint of Elsevier, Inc. All rights reserved.

fi·brin·o·pep·tide

(fī'brin-ō-pep'tīd),
One of two pairs of peptides (A and B) released from the amino-terminal ends of 2α- (or Aα-) and 2β- (or Bβ-)chains of fibrinogen by the action of thrombin to form fibrin; they have a vasoconstrictive effect.
Farlex Partner Medical Dictionary © Farlex 2012

fi·brin·o·pep·tide

(fī'brin-ō-pep'tīd)
One of two pairs of peptides (A and B) released from the amino-terminal ends of 2α- and 2β-chains of fibrinogen by the action of thrombin to form fibrin; has a vasoconstrictive effect.
Medical Dictionary for the Health Professions and Nursing © Farlex 2012
References in periodicals archive ?
(1989) Circadian variation of plasma fibrinopeptide A level in patients with variant angina.
In a repeatability test of a simple 3 peptide sample, two quantifiable peptides (Angiotensin III and Fibrinopeptide B) had an intensity CV [less than or equal to] 15%.
Fibrinopeptide A level and left ventricular ejection fraction were the only independent predictors of cardiac death (J.
Dyr, "Fibrinopeptides A and B release in the process of surface fibrin formation," Blood, vol.
Congenital dysfibrinogenemia characterized by defective release of fibrinopeptide A and fibrinogen degradation products.
This defect is caused by impaired thrombin-mediated release of fibrinopeptide A and/or fibrinopeptide B from fibrinogen, as well as impaired fibrin monomer polymerization.
Thrombin-mediated release of fibrinopeptide A (FPA) and FPB from the N-termini of the A[alpha]- and B[beta]-chains, respectively, results in the formation of fibrin monomer [([alpha], [beta], [gamma]).sub.2].
(54) proposed a proteomic pattern of 22 polypeptides with high diagnostic sensitivity and specificity for urothelial cancer and highlighted fibrinopeptide A as a potential diagnostic biomolecule.
The enzyme is thrombin-like in nature and hydrolyzes fibrinopeptide A from the intact fibrinogen molecule, unlike thrombin, which hydrolyzes fibrinopetide A and B from fibrinogen.
Clot formation includes the activation of platelets, as denoted by the release of P-selectin and thrombosis, resulting in fibrinopeptide A.
The extension is modeled after fibrinopeptide B to facilitate renal filtration, contains D-amino acids to prevent proteolytic breakdown, and can eventually be released from the partially degraded substrates by photocleavage to generate a reporter with fixed molecular mass.