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