A. Henschen & B. Henssel 
Structural variants and interactions [PDF ebook] 
Stockholm, Sweden, July 9–10, 1983

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