Fibrinogen – Blutgerinnungsfaktor I Biochemische Aspekte

• LITERATUR

• 1 Alving B, Murano G, Walz D. Partial chemical characterization of S-carboxymethylated chains of rabbit fibrin(ogen): Evidence for separate chain biosynthesis. Thrombos. Haemostas 1977; 38: 26
• 2 Birken S, Wilner G. D, Canfield R. E. Studies of the structure of canine fibrinogen. Thromb. Res 1975; 7: 599
• 3 Blombäck B. Studies on the action of thrombic enzymes on bovine fibrinogen as measured by N-terminal analysis. Arkiv Kemi 1958; 12: 321
• 4 Blombäck B, Blombäck M. Purification of human and bovine fibrinogen. Arkiv Kemi 1956; 10: 415
• 5 Blombäck B, Yamashina I. On the N-terminal amino acids in fibrinogen and fibrin. Arkiv Kemi 1958; 12: 299
• 6 Blombäck B, Blombäck M, Edman P, Hessel B. Human Fibrinopeptides: Isolation, characterization and structure. Biochim. Bio-phys. Acta 1966; 115: 371
• 7 Blombäck M, Blombäck B, Mammen E. F, Prasad A. S. Fibrinogen Detroit-a molecular defect in the N-terminal disulphide knot of human fibrinogen?. Nature 1968; 218: 134
• 8 Blombäck B, Gröndahl N. J, Hessel B, Iwanaga S, Wallen P. Primary structure of human fibrinogen and fibrin. II. Structural studies on NH₂-terminal part of γ-chain. J. Biol. Chem 1973; 248: 5806
• 9 Blombäck B, Hessel B, Hogg D. Disulfide bridges in NH₂-terminal part of human fibrinogen. Thromb. Res 1976; 8: 639
• 10 Collen D, Kudryk B, Hessel B, Blombäck B. Primary structure of human fibrinogen and fibrin. Isolation and partial characterization of chains of fragment D. J. Biol. Chem 1975; 250: 5808
• 11 Cottrell B, Doolittle R. F. The amino acid sequence of a 27-residue peptide released from the A-chain carboxy-terminus during the plasmic digestion of human fibrinogen. Biochem. Biophys. Res. Comm 1976; 71: 754
• 12 Dayhoff M. O. Atlas of protein sequence and structure. 5. National Biomedical Research Foundation 1972
• 13 Didisheim P, Lewis J. H. Fibrinolytic and coagulant activities of certain snake venoms and proteases. Proc. Soc. Exptl. Biol. Med 1956; 93: 10
• 14 Doolittle R. F, Watt K. W. K, Cottrell B. A, Strong D. D, Riley M. The amino acid sequence of the A-chain of human fibrinogen. Nature 1979; 280: 464
• 15 Edman P, Henschen A. Sequence determination. In: Needleman S. B. (Ed.): Protein sequence determination 2. Ed.. Springer; Berlin: 1975: 232
• 16 Von Feiten A, Frick P. G, Straub P. W. Studies on fibrin monomer aggregation in congenital dysfibrinogenaemia (Fibrinogen »Zürich«): Separation of a pathological from a normal fibrin fraction. Brit. J. Haematol 1969; 16: 353
• 17 Francis C. W, Marder V. J, Martin S. E. Demonstration of a large molecular weight variant of the γ-chain of normal human plasma fibrinogen. J. Biol. Chem 1980; 255: 5599
• 18 Gårdlund B, Hessel B, Marguerie G, Murano G, Blombäck B. Primary structure of human fibrinogen. Characterization of disul-fide-containing cyanogen-bromide fragments. Eur. J. Biochem 1977; 77: 595
• 19 Gollwitzer R, Bode W, Schramm H. J, Typke D, Guckenberger R. Paracrystalline structure of native human fibrinogen. In: Peeters H. (Ed.) Protides of biological fluids 1980; 28: 307
• 20 Hall C. E, Slayter H. S. The fibrinogen molecule: Its size, shape and mode of polymerisation. J. Biophys. Biochem. Cytol 1959; 5: 11
• 21 Haverkate F, Timan G. Protective effect of calcium in the plasmin degradation of fibrinogen and fibrin fragments D. Thromb. Res 1977; 10: 803
• 22 Henschen A. Number and reactivity of disulfide bonds in fibrinogen and fibrin. Arkiv Kemi 1964; 22: 355
• 23 Henschen A. Disulfide bridges in the middle part of human fibrinogen. Hoppe-Seyler’s Z. Physiol. Chem 1978; 359: 1757
• 24 Henschen A, Edman P. Large scale preparation of S-carboxymethylated chains of human fibrin and fibrinogen and the occurrence of γ-chain variants. Biochim. Biophys. Acta 1972; 263: 351
• 25 Henschen A, Lottspeich F. Amino acid sequence of human fibrin. Preliminary note on the completion of the B-chain sequence. Hoppe-Seyler’s Z. Physiol. Chem 1977; 358: 1643 a
• 26 Henschen A, Lottspeich F. Sequence homology between γ-chain and ß-chain in human fibrin. Thromb. Res 1977; b 11: 869
• 27 Henschen A, Southan C. Methode zur Isolierung abnormer Fibrinogene aus Plasma. In: Deutsch E, Lechner K. (Eds.): Fibrinolyse, Thrombose, Hämostase Schattauer; Stuttgart: 1980: 290
• 28 Henschen A, Lottspeich F, Hessel B. Amino acid sequence of human fibrin. Preliminary note on the completion of the intermediate part of the A-chain sequence. Hoppe-Seyler’s Z. Physiol. Chem 1979; 360: 1951
• 29 Herzig R. H, Ratnoff O. D, Shainoff J. R. Studies on a procoagulant fraction of southern copperhead snake venom: the preferential release of fibrinopeptide B. J. Lab. Clin. Med 1970; 76: 451
• 30 Hessel B. On the structure of the COOH-terminal part of the AA-chain of human fibrinogen. Thromb. Res 1975; 7: 75
• 31 Iwanaga S, Henschen A, Blombäck B. On the primary structure of human fibrinogen. I. Two-dimensional »Finger Prints« of tryp-tic digests of sulfitolyzed fibrinogen and fibrin. Acta Chem. Scand 1966; 20: 1183
• 32 Jevons F. R. Tyrosine O-sulphate in fibrinogen and fibrin. Biochem. J 1963; 89: 621
• 33 Kazal L. A, Amsel S, Miller O. P, Tocantins L. M. The preparation and some properties of fibrinogen precipitated from human plasma by glycine. Proc. Soc. Exptl. Biol. Med 1963; 113: 989
• 34 Laki K. The polymerization of proteins: the action of thrombin on fibrinogen. Arch. Biochem. Biophys 1951; 32: 317
• 35 Lottspeich F, Henschen A. Amino acid sequence of human fibrin. Preliminary note on the completion of the γ-chain sequence. Hoppe-Seyler’s Z. Physiol. Chem 1977; 358: 935
• 36 Marder V. J, Budzynski A. Z, James H. L. High molecular weight derivatives of human fibrinogen produced by plasmin. III. Their NH ₂-terminal amino acids and comparison with the »NH₂-terminal disulfide knot«. J. Biol. Chem 1972; 247: 4775
• 37 Marx R, Schramm W. Diskussionsbeitrag zum Thema »Fibrinogenopathien«. In: Schimpf K. (Ed.) Fibrinogen, Fibrin und Fibrinkleber Schattauer; Stuttgart: 1980: 195
• 38 Pirkle H, Henschen A, Potapous A. Interspecies constancy of N-terminal amino-acid sequences in the γ-chain of fibrinogen. Nature 1969; 223: 400
• 39 Sharp J. J, Cassman K. G, Doolittle R. F. Amino acid sequence of the carboxy-termi-nal cyanogen bromide fragment from bovine and human fibrinogen γ-chains. FEBS Letters 1972; 25: 334
• 40 Soria J, Soria C, Boulard C. Anomalie de structure du fibrinogène »Metz« localisée sur la chaîne a (A) de la molecule. Biochimie 1972; 54: 415
• 41 Takagi T, Doolittle R. F. Amino acid sequence studies on plasmin-derived fragments of human fibrinogen: Amino-terminal sequences of intermediate and terminal fragments. Biochemistry 1975; 14: 940 a
• 42 Takagi T, Doolittle R. Amino acid sequence studies on the A-chain of human fibrinogen. Location of four plasmin attack points and a covalent cross-linking site. Biochemistry 1975; b 14: 5149
• 43 Timpl R, Fietzek P. P, Wachter E, Van Delden V. Disulfide-linked cyanogen bromide peptides of bovine fibrinogen. II. Isolation and sequence analysis of the chain constituents from the amino terminal region. Bio-chim. Biophys. Acta 1977; 490: 420
• 44 Töpfer-Petersen E. Kohlehydratseitenketten im Fibrinogen. In: Schimpf K. (Ed.): Fibrinogen, Fibrin und Fibrinkleber Schattauer; Stuttgart: 1980: 43
• 45 Töpfer-Petersen E, Henschen A. Carbohydrate carrying peptides isolated from bovine fibrin B- and γ-chain. Thromb. Res 1977; 11: 881
• 46 Töpfer-Petersen E, Lottspeich F, Henschen A. Carbohydrate linkage site in the B-chain of human fibrin. Hoppe-Seyler’s Z. Physiol. Chem 1976; 357: 1509
• 47 Tooney N. M, Cohen C. Crystalline states of a modified fibrinogen. J. Mol. Biol 1977; 110: 363
• 48 Witt I. Biochemie der Blutgerinnung und Fibrinolyse. Verlag Chemie; Weinheim: 1975
• 49 Witt L, Hasler K. Influence of organically bound phosphorus in foetal and adult fibrinogen on the kinetics of the interaction between thrombin and fibrinogen. Biochim. Biophys. Acta 1972; 271: 357
• 50 Wolfenstein-Todel C, Mosesson M. W. Human plasma fibrinogen heterogeneity: Evidence for an extended carboxyl-terminai sequence in a normal γ-chain variant (γ’). Proc. Natl. Acad. Sci. USA 1980; 77: 5069