Fibrinogen--structure, functional aspects, metabolism proceedings by Workshop on Fibrinogen (1982 Leiden, Netherlands)

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Edition Notes

Includes bibliographical references and index.

Book details

StatementWorkshop on Fibrinogen, May 12-14, 1982, Leiden, The Netherlands ; editors, F. Haverkate ... [et al.].
ContributionsHaverkate, F. 1931-
LC ClassificationsQP93.5 .W67 1982
The Physical Object
Paginationxvi, 343 p. :
Number of Pages343
ID Numbers
Open LibraryOL3503276M
ISBN 103110089866
LC Control Number82023635

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Journal of Vascular and Interventional Radiology, 12(6), N2 - Fibrinogen plays a central role in the mechanism of coagulation and thrombosis and is partially involved in the development of postintervention restenosis.

Because of therapeutic implications, it is convenient Cited by: 1. Author(s): Haverkate,F(Frits),; Workshop on Fibrinogen,( Leiden, Netherlands) Title(s): Fibrinogen, structure, functional aspects, metabolism. As illustrated in Figure 2, each arm of the fibrinogen molecule contains single Aα, Bβ, and γ chains from each of the three pairs of polypeptide chains.

The central domain is a dimeric structure in which each dimer contains the three amino terminals of the individual by: Fibrinogen, originally factor I (FI) in the clotting cascade, is a fibrous adhesive glycoprotein, present in the plasma at a concentration of approximately g/L, which is essential for platelet aggregation and for fibrin gel formation in hemostasis, wound healing, inflammation, angiogenesis, and.

Fibrinogen is a naturally occurring plasma protein ( kDa, globular) that functions as a major element in the coagulation cascade, contributing to clot formation and wound healing.

Fibrinogen has also been defined as fibrin molecules coupled to charged by: Fibrin Formation, Structure and Properties. including some basic aspects of clotting, fibrinolysis, and molecular origins of fibrin mechanical properties. Fig.

Fibrinogen structure. Zinc binding to fibrinogen and fibrin was studied by two techniques. Scatchard analysis of ultrafiltration eluates reveals that fibrinogen has multiple Zn(II)-binding sites, K D (fibrinogen) = 18 μ m; n = by: Until now, the area of drug metabolism and pharmacokinetics has been lacking in texts written for the Medicinal Chemist.

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15, No.): Medicine & Health Science Books @ A latex metabolism book of fibrin/fibrinogen degradation products in plasma using metabolism book monoclonal antibody Author links open overlay panel Massoud Mirshahi a b c Jeannette Soria a b c Claudine Soria a b c Jean-Yves Perrot a b c Claude Boucheix a b cCited by: Fibrinogen Structure - Functional Aspects - Metabolism Proceedings - Workshop on Fibrinogen MayLeiden, The Netherlands Editors F.

Haverkate - A. Menschen - W. Nieuwenhuizen P.W. In: Haverkate F, Henschen A, Nieuwenhuizen W, Straub PW (ed) Fibrinogen structure, functional aspects, metabolism, de Gruyter, Hawthorne, pp – Google Scholar Francis JL, Simmonds VJ, Armstrong DJ () Fibrinogen bound sialic acid and liver sialic transferase activity in an experimental animal model of : E.

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The focus is on new topics regarding the functional interaction between multiple enzymes and the initiation process of starch biosynthesis, which are essential for further understanding of related metabolic features. Fibrin is normally present in an inactive form known as fibrinogen.

Fibrinogen is soluble in water and is found in high concentrations in the blood, where it waits until needed to form a clot. When given the signal, fibrinogen is converted to fibrin, which then assembles into an extended network of fibers.

[Fibrinogen: structure, function and interaction with proteins and cells]. [Article in German] The dimerous three-chained protein fibrinogen has at its disposal different functional zones which are included in the process of polymerisation and which possess importance for the specific reaction of fibrinogen with certain cells.

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The region of a protein that associates with a ligand, known as the ligand’s binding site, usually consists of a cavity in the protein surface formed by a particular arrangement of amino acids. These amino acids can belong to different portions of the polypeptide chain that are brought together when the protein folds (Figure ).Separate regions of the protein surface generally provide.

Semin Thromb Hemost. ;24(2) Fibrinogen structure and fibrin clot assembly. Mosesson MW(1). Author information: (1)University of Wisconsin Medical School, Sinai Samaritan Medical Center, MilwaukeeUSA. Fibrinogen is a complex multifunctional protein, which contains constitutive association sites (gammaXL, D:D, Da, Db) as well as cryptic sites that become exposed as a Cited by:   Vitamins is aimed at nutritionists, biochemists, physiologists and physicians whether they be researchers, teachers or students.

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Furthermore, hemodilution, hypothermia, and acidosis influence fibrinogen concentrations and metabolism. The role of fibrinogen as a driver of trauma induced coagulopathy has focused on studies quantifying fibrinogen concentration.

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Functional aspects of these proteins, including metabolite transport, have been reviewed by Dr. Ferdinando Palmieri and Dr. Ciro Leonardo Pierri ().

Diseases caused by defects of mitochondrial carriers are reviewed by Palmieri et al. () and by Gutiérrez-Aguilar and Baines InterPro: IPR The enzymes involved in metabolism are present in many tissues but generally are more concentrated in the liver. Drug metabolism rates vary among patients.

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