Structural variants and interactions

ISBN-13: 9783110098068 / Niemiecki / Twarda / 1986 / 430 str.

Max-Planck-Institut Für Biochemie

Spis treści

Frontmatter -- Preface -- Contents -- I. A HISTORICAL NOTE -- Two thousand years of fibrinogen research and evidence for fibrin being the first protein -- II. GENE ANALYSIS -- Fibrinogen evolution - The structure and evolution of fibrinogen: The coiled coil region -- Absence of gross defect of fibrinogen genes in one patient with congenital afibrinogenemia -- III. FIBRINOGEN-FIBRIN CONVERSION -- Fibrinogen to fibrin - an overview -- Fibrin - specific monoclonal antibodies are elicited by immunization with a synthetic fibrin-like peptide -- Enhancement of fibrin polymerization by active site - inhibited thrombin -- Peptides released from human fibrinogen by thrombic enzymes -- The analysis of fibrinopeptide release from S--carboxymethylated fibrinogen chains using high-performance liquid chromatography -- Moaification of the fibrin a-chain by dipeptidyl peptidase IV -- IV. FIBRINOGEN-FIBRIN INTERACTION -- Analysis of composition of soluble fibrinogen/fibrin complexes by differential ultracentrifugation -- Reversible interactions of fibrin and fibrinogen: an ultracentrifugation study -- V. NORMAL FIBRINOGEN VARIANTS -- Evidence that the amount of heparin precipitable fraction is influenced by fibrinogen quality -- The location of a second in vivo phosphorylation site in the Aa-chain of human fibrinogen -- Evidence that the y chain population of human platelet fibrinogen lacks the y' variant that is present in plasma fibrinogen -- Differences and similarities between human adult and fetal fibrinogen fragments D1 -- VI. ABNORMAL FIBRINOGEN VARIANTS -- Functional defects in abnormal fibrinogens -- Study of 10 cases of congenital dysfibrinogenemia: clinical and molecular biological aspects -- Fibrinogens Sydney I and II, a kinetic study of (His16 )FPA cleavage and its effect on FPB cleavage -- Fibrinogens London I - IV, Manchester, Sydney I and II. Cleavage of fibrinopeptides by thrombin and expression of their polymerisation abnormalities -- Aspects of evaluation of fibrinogen Stony Brook - A defect resulting in failure to release fibrinopeptide A -- Fibrinogen Tokyo II: An abnormal fibrinogen with an impaired polymerization site on the aligned DD domain of fibrin molecules -- Fibrinogen Milan II: A congenital dysfibrinogenemia with a defective clotting by thrombin, normal clotting by arvin, reptilase and prothrombin-staphy1ocoagulase complex, associated with thrombotic episodes -- Preliminary report concerning two new cases of congenital dysfibrinogenemia (Homburg II and Homburg III) -- The effect of sodium citrate on fibrin polymerisation in patients with liver disease -- VII. FIBRINOGEN DEGRADATION PRODUCTS -- Studies of the proteolytic fragments of the C-terminal portion of the a-chain of human fibrinogen -- Biodistribution or human fibrinogen-derived peptides in rabbits -- Structure-function studies on a vasoactive pentapeptide derived from plasm in degradation of human fibrin(ogen) -- Purification and characteristics of a vasoactive peptide derived from elastase degradation of human fibrin(ogen) -- Relation of crosslinked to non crosslinked fibrin derivatives in tumor ascites compared to cirrhosis ascites -- VIII. INTERACTION WITH PLASMINOGEN AND ITS ACTIVATOR -- Study of the interaction between plasminogen and fibrinogen degradation products using immunoenzymological assay -- Fibrin and plasminogen structures involved in the tissue-type plasminogen activator catalyzed activation of plasminogen -- Kinetics of the tissue-type plasminogen activatormediated activation of plasminogen. Influence of CNBr fibrin(ogen) fragment FCB-2 and different forms of plasminogen -- IX. INTERACTION WITH CELLS -- Structural characterization of the recognition site for platelet receptors on human fibrinogen -- Binding or fibrinogen to ADP-treated platelets: Importance of the A?-chain -- Inhibition of fibrinogen binding to activated platelets by oligoamines -- Specific interaction between fibrinogen-fibrin and endothelial cells -- Influence of fibr