메뉴 건너뛰기




Volumn 79, Issue 1, 2000, Pages 561-583

Polymerization of rod-like macromolecular monomers studied by stopped- flow, multiangle light scattering: Set-up, data processing, and application to fibrin formation

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; FIBRIN FORMATION; INFORMATION PROCESSING; LIGHT SCATTERING; POLYMERIZATION; PROTEIN ANALYSIS; PROTEIN STRUCTURE; QUALITY CONTROL; STRUCTURE ANALYSIS;

EID: 0033917886     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76317-X     Document Type: Article
Times cited : (36)

References (74)
  • 1
    • 0020446337 scopus 로고
    • Kinetics of formation of fibrin oligomers. II. Size distributions of ligated oligomers
    • Bale, M. D., P. A. Janmey, and J. D. Ferry. 1982. Kinetics of formation of fibrin oligomers. II. Size distributions of ligated oligomers. Biopolymers. 21:2265-2277.
    • (1982) Biopolymers , vol.21 , pp. 2265-2277
    • Bale, M.D.1    Janmey, P.A.2    Ferry, J.D.3
  • 2
    • 0027937766 scopus 로고
    • Fibrin structures during tissue-type plasminogen activator-mediated fibrinolysis studied by laser light scattering: Relation to fibrin enhancement of plasminogen activation
    • Bauer, R., S. L. Hansen, G. Jones, E. Suenson, S. Thorsen, and L. Øgendal. 1994. Fibrin structures during tissue-type plasminogen activator-mediated fibrinolysis studied by laser light scattering: relation to fibrin enhancement of plasminogen activation. Eur. Biophys. J. 23:239-252.
    • (1994) Eur. Biophys. J. , vol.23 , pp. 239-252
    • Bauer, R.1    Hansen, S.L.2    Jones, G.3    Suenson, E.4    Thorsen, S.5    Øgendal, L.6
  • 3
    • 0343243681 scopus 로고
    • On the nature of the conversion of fibrinogen to fibrin
    • Belitzer, W. A., and J. L. Chodorova. 1952. On the nature of the conversion of fibrinogen to fibrin. Biochimija (USSR). 17:676-683.
    • (1952) Biochimija (USSR) , vol.17 , pp. 676-683
    • Belitzer, W.A.1    Chodorova, J.L.2
  • 4
    • 33947462664 scopus 로고
    • Light scattering from non-Gaussian chains
    • Benoit, H., and P. Doty. 1953. Light scattering from non-Gaussian chains. J. Phys. Chem. 57:958-963.
    • (1953) J. Phys. Chem. , vol.57 , pp. 958-963
    • Benoit, H.1    Doty, P.2
  • 6
    • 0030199185 scopus 로고    scopus 로고
    • Fibrinogen and fibrin - Proteins with complex roles in hemostasis and thrombosis
    • Blombäck, B. 1996. Fibrinogen and fibrin - proteins with complex roles in hemostasis and thrombosis. Thromb. Res. 83:1-75.
    • (1996) Thromb. Res. , vol.83 , pp. 1-75
    • Blombäck, B.1
  • 7
    • 0017201715 scopus 로고
    • Fibrin formation: The role of the fibrinogen-fibrin monomer complex
    • Brass, E. P., W. B. Forman, R. V. Edwards, and O. Lindan. 1976. Fibrin formation: the role of the fibrinogen-fibrin monomer complex. Thromb. Heamost. 36:37-48.
    • (1976) Thromb. Heamost. , vol.36 , pp. 37-48
    • Brass, E.P.1    Forman, W.B.2    Edwards, R.V.3    Lindan, O.4
  • 8
    • 0018777009 scopus 로고
    • The fibrin-solubilizing effect of fibrinogen as studied by light scattering
    • Brosstad, F., P. Kierulf, and H. C. Godal. 1979. The fibrin-solubilizing effect of fibrinogen as studied by light scattering. Thromb. Res. 14: 705-712.
    • (1979) Thromb. Res. , vol.14 , pp. 705-712
    • Brosstad, F.1    Kierulf, P.2    Godal, H.C.3
  • 9
    • 0017601513 scopus 로고
    • Mass-length ratio of fibrin fibers from gel permeation and light scattering
    • Carr, M. E., Jr., L. L. Shen, and J. Hermans. 1977. Mass-length ratio of fibrin fibers from gel permeation and light scattering. Biopolymers. 16:1-15.
    • (1977) Biopolymers , vol.16 , pp. 1-15
    • Carr M.E., Jr.1    Shen, L.L.2    Hermans, J.3
  • 10
    • 36849118179 scopus 로고
    • Light scattering from very long rod-like particles and an application to polymerized fibrinogen
    • Casassa, E. F. 1955. Light scattering from very long rod-like particles and an application to polymerized fibrinogen. J. Chem. Phys. 23:596-597.
    • (1955) J. Chem. Phys. , vol.23 , pp. 596-597
    • Casassa, E.F.1
  • 12
    • 0021118122 scopus 로고
    • Fibrinogen and fibrin
    • Doolittle, R. F. 1984. Fibrinogen and fibrin. Anna. Rev. Biochem. 53: 195-229.
    • (1984) Anna. Rev. Biochem. , vol.53 , pp. 195-229
    • Doolittle, R.F.1
  • 13
    • 0014672070 scopus 로고
    • Thiol-disulfide interchange reactions between serum albumin and disulfides
    • Edwards, F. B., R. B. Rombauer, and B. J. Campbell. 1969. Thiol-disulfide interchange reactions between serum albumin and disulfides. Biochim. Biophys. Acta. 194:234-245.
    • (1969) Biochim. Biophys. Acta , vol.194 , pp. 234-245
    • Edwards, F.B.1    Rombauer, R.B.2    Campbell, B.J.3
  • 14
    • 85031592854 scopus 로고
    • Electron microscopy of fibrinogen, its plasmic fragments and small polymers
    • M. W. Mosesson and R. F. Doolittle, editors. Annals of the New York Academy of Sciences, New York
    • Erickson, H. P., and W. E. Fowler. 1983. Electron microscopy of fibrinogen, its plasmic fragments and small polymers. In Molecular Biology of Fibrinogen and Fibrin. M. W. Mosesson and R. F. Doolittle, editors. Annals of the New York Academy of Sciences, Vol. 406. New York. 146-163.
    • (1983) Molecular Biology of Fibrinogen and Fibrin , vol.406 , pp. 146-163
    • Erickson, H.P.1    Fowler, W.E.2
  • 15
    • 0032537486 scopus 로고    scopus 로고
    • Crystal structure of fragment double-D from human fibrin with two different bound ligands
    • Everse, S. J., G. Spraggon, L. Veerapandian, M. Riley, and R. F. Doolittle. 1998. Crystal structure of fragment double-D from human fibrin with two different bound ligands. Biochemistry. 37:8637-8642.
    • (1998) Biochemistry , vol.37 , pp. 8637-8642
    • Everse, S.J.1    Spraggon, G.2    Veerapandian, L.3    Riley, M.4    Doolittle, R.F.5
  • 16
    • 0001395438 scopus 로고
    • The mechanism of polymerization of fibrinogen
    • Ferry, J. D. 1952. The mechanism of polymerization of fibrinogen. Proc. Natl. Acad. Sci. USA. 38:566-569.
    • (1952) Proc. Natl. Acad. Sci. USA , vol.38 , pp. 566-569
    • Ferry, J.D.1
  • 17
    • 0004986839 scopus 로고
    • Molecular size distribution in linear condensation polymers
    • Flory, P. J. 1936. Molecular size distribution in linear condensation polymers. J. Am. Chem. Soc. 58:1877-1885.
    • (1936) J. Am. Chem. Soc. , vol.58 , pp. 1877-1885
    • Flory, P.J.1
  • 18
    • 0242497763 scopus 로고
    • Kinetics of the degradation of polyesters by alcohols
    • Flory, P. J. 1940. Kinetics of the degradation of polyesters by alcohols. J. Am. Chem. Soc. 62:2255-2261.
    • (1940) J. Am. Chem. Soc. , vol.62 , pp. 2255-2261
    • Flory, P.J.1
  • 19
    • 0343243649 scopus 로고
    • Molecular size distribution in linear condensation polymers
    • correction
    • Flory, P. J. 1942. Molecular size distribution in linear condensation polymers. J. Am. Chem. Soc. 64:3067 (correction).
    • (1942) J. Am. Chem. Soc. , vol.64 , pp. 3067
    • Flory, P.J.1
  • 21
    • 0242669147 scopus 로고
    • Refractive index as a function of wavelength for sixty API-NBS hydrocarbons
    • Forziati, A. F. 1950. Refractive index as a function of wavelength for sixty API-NBS hydrocarbons. J. Res. Natl. Bur. Stan. 44:373-385.
    • (1950) J. Res. Natl. Bur. Stan. , vol.44 , pp. 373-385
    • Forziati, A.F.1
  • 22
    • 0000978736 scopus 로고
    • Density, refractive index, boiling point and vapor pressure of eight monoolefin (1-alkene), six pentadiene and two cyclomonoolefin hydrocarbons
    • Forziati, A. F., D. L. Camin, and F. D. Rossini. 1950. Density, refractive index, boiling point and vapor pressure of eight monoolefin (1-alkene), six pentadiene and two cyclomonoolefin hydrocarbons. J. Res. Natl. Bur. Stan. 45:406-410.
    • (1950) J. Res. Natl. Bur. Stan. , vol.45 , pp. 406-410
    • Forziati, A.F.1    Camin, D.L.2    Rossini, F.D.3
  • 24
    • 0008323778 scopus 로고
    • Application of light scattering to biological systems
    • Geiduschek, E. P., and A. M. Holtzer. 1958. Application of light scattering to biological systems. Adv. Biol. Med. Phys. 6:431-551.
    • (1958) Adv. Biol. Med. Phys. , vol.6 , pp. 431-551
    • Geiduschek, E.P.1    Holtzer, A.M.2
  • 26
    • 70249091771 scopus 로고
    • The fibrinogen molecule: Its size, shape and mode of polymerization
    • Hall, C. E., and H. S. Slayter. 1959. The fibrinogen molecule: its size, shape and mode of polymerization. J. Biophys. Biochem. Cytol. 5:11-17.
    • (1959) J. Biophys. Biochem. Cytol. , vol.5 , pp. 11-17
    • Hall, C.E.1    Slayter, H.S.2
  • 27
    • 0018597469 scopus 로고
    • Assembly of fibrin. A light scattering study
    • Hantgan, R. R., and J. Hermans. 1979. Assembly of fibrin. A light scattering study. J. Biol. Chem. 254:11272-11281.
    • (1979) J. Biol. Chem. , vol.254 , pp. 11272-11281
    • Hantgan, R.R.1    Hermans, J.2
  • 30
    • 0020452574 scopus 로고
    • Kinetics of formation of fibrin oligomers. I. Theory
    • note that, in this paper, ref. 14 is incorrect
    • Janmey, P. A. 1982. Kinetics of formation of fibrin oligomers. I. Theory. Biopolymers. 21:2253-2264. (note that, in this paper, ref. 14 is incorrect).
    • (1982) Biopolymers , vol.21 , pp. 2253-2264
    • Janmey, P.A.1
  • 31
    • 0021054115 scopus 로고
    • Polymerization of fibrin: Analysis of light-scattering data and relation to a peptide release
    • Janmey, P. A., M. D. Bale, and J. D. Ferry. 1983a. Polymerization of fibrin: analysis of light-scattering data and relation to a peptide release. Biopolymers. 22:2017-2019.
    • (1983) Biopolymers , vol.22 , pp. 2017-2019
    • Janmey, P.A.1    Bale, M.D.2    Ferry, J.D.3
  • 32
    • 0021115863 scopus 로고
    • Kinetics of fibrin oligomer formation observed by electron microscopy
    • Janmey, P. A., L. Erdile, M. D. Bale, and J. D. Ferry. 1983b. Kinetics of fibrin oligomer formation observed by electron microscopy. Biochemistry. 22:4336-4340.
    • (1983) Biochemistry , vol.22 , pp. 4336-4340
    • Janmey, P.A.1    Erdile, L.2    Bale, M.D.3    Ferry, J.D.4
  • 33
    • 0019808032 scopus 로고
    • Analysis of human fibrin-opeptides by high-performance liquid chromatography
    • Kehl, M., F. Lottspeich, and A. Henshen. 1981. Analysis of human fibrin-opeptides by high-performance liquid chromatography. Hoppe-Seyler's Z. Physiol. Chem. 362:1661-1664.
    • (1981) Hoppe-Seyler's Z. Physiol. Chem. , vol.362 , pp. 1661-1664
    • Kehl, M.1    Lottspeich, F.2    Henshen, A.3
  • 34
    • 0021213469 scopus 로고
    • Characterization of soluble polymerized fibrin formed in the presence of excess fibrinogen fragment D
    • Knoll, D., R. R. Hantgan, J. Williams, J. McDonagh, and J. Hermans. 1984. Characterization of soluble polymerized fibrin formed in the presence of excess fibrinogen fragment D. Biochemistry. 23:3708-3715.
    • (1984) Biochemistry , vol.23 , pp. 3708-3715
    • Knoll, D.1    Hantgan, R.R.2    Williams, J.3    McDonagh, J.4    Hermans, J.5
  • 35
    • 0021995951 scopus 로고
    • A monoclonal antibody, specific for human fibrinogen, fibrinopeptide A-containing fragments and not reacting with free fibrinopeptide A
    • Koppert, P. W., C. M. G. Huijsmans, and W. Nieuwenhuizen. 1985. A monoclonal antibody, specific for human fibrinogen, fibrinopeptide A-containing fragments and not reacting with free fibrinopeptide A. Blood. 66:503-507.
    • (1985) Blood , vol.66 , pp. 503-507
    • Koppert, P.W.1    Huijsmans, C.M.G.2    Nieuwenhuizen, W.3
  • 36
    • 0001096593 scopus 로고
    • Light scattering of stiff chain polymers
    • Koyama. R. 1973. Light scattering of stiff chain polymers. J. Phys. Soc. Jpn. 34:1029-1038.
    • (1973) J. Phys. Soc. Jpn. , vol.34 , pp. 1029-1038
    • Koyama, R.1
  • 37
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 39
    • 0000852842 scopus 로고
    • On the significance of the release of two different peptides from fibrinogen during clotting
    • Laurent, T. C., and B. Blombäck. 1958. On the significance of the release of two different peptides from fibrinogen during clotting. Acta Chem. Scand. 12:1875-1877.
    • (1958) Acta Chem. Scand. , vol.12 , pp. 1875-1877
    • Laurent, T.C.1    Blombäck, B.2
  • 40
    • 0343243639 scopus 로고
    • Small angle X-ray scattering measurements with dilute solutions of bovine fibrinogen
    • Lederer, K. 1972. Small angle X-ray scattering measurements with dilute solutions of bovine fibrinogen. J. Mol. Biol. 63:315-320.
    • (1972) J. Mol. Biol. , vol.63 , pp. 315-320
    • Lederer, K.1
  • 41
    • 0029950081 scopus 로고    scopus 로고
    • Transient intermediates in the thrombin activation of fibrinogen. Evidence for only the desAA species
    • Li, X., D. Galanakis, and D. A. Gabriel. 1996. Transient intermediates in the thrombin activation of fibrinogen. Evidence for only the desAA species. J. Biol. Chem. 271:11767-11771.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11767-11771
    • Li, X.1    Galanakis, D.2    Gabriel, D.A.3
  • 42
    • 0018960498 scopus 로고
    • Steady-state kinetic study of the bovine thrombin-fibrinogen interaction
    • Martinelli, R. A., and H. A. Scheraga. 1980. Steady-state kinetic study of the bovine thrombin-fibrinogen interaction. Biochemistry. 19: 2343-2350.
    • (1980) Biochemistry , vol.19 , pp. 2343-2350
    • Martinelli, R.A.1    Scheraga, H.A.2
  • 43
    • 0023947560 scopus 로고
    • Mechanism of fibrin coagulation based on selective, cation-driven, protofibril association
    • Marx, G. 1988. Mechanism of fibrin coagulation based on selective, cation-driven, protofibril association. Biopolymers. 27:763-774.
    • (1988) Biopolymers , vol.27 , pp. 763-774
    • Marx, G.1
  • 44
    • 0021110096 scopus 로고
    • Structural organization of the C-terminal parts of fibrinogen Aα-chains
    • Medved', L. V., O. V. Gorkun, and P. L. Privalov. 1983. Structural organization of the C-terminal parts of fibrinogen Aα-chains. FEBS Lett. 160:291-295.
    • (1983) FEBS Lett. , vol.160 , pp. 291-295
    • Medved', L.V.1    Gorkun, O.V.2    Privalov, P.L.3
  • 45
    • 0021905372 scopus 로고
    • The role of fibrinogen αC-domains in the fibrin assembly process
    • Medved', L. V., O. V. Gorkun, V. F. Manyakov, and V. A. Belitser. 1985. The role of fibrinogen αC-domains in the fibrin assembly process. FEBS Lett. 181:109-112.
    • (1985) FEBS Lett. , vol.181 , pp. 109-112
    • Medved', L.V.1    Gorkun, O.V.2    Manyakov, V.F.3    Belitser, V.A.4
  • 46
    • 0025679015 scopus 로고
    • Electron microscope investigation of the early stages of fibrin assembly. Twisted protofibrils and fibers
    • Medved', L. V., T. Ugarova, Y. Veklich, N. Lukinova, and J. W. Weisel. 1990. Electron microscope investigation of the early stages of fibrin assembly. Twisted protofibrils and fibers. J. Mol. Biol. 216:503-509.
    • (1990) J. Mol. Biol. , vol.216 , pp. 503-509
    • Medved', L.V.1    Ugarova, T.2    Veklich, Y.3    Lukinova, N.4    Weisel, J.W.5
  • 47
    • 0014223584 scopus 로고
    • Physicochemical studies of bovine fibrinogen. IV. Ultraviolet absorption and its relation to the structure of the molecule
    • Mihalyi, M. 1968. Physicochemical studies of bovine fibrinogen. IV. Ultraviolet absorption and its relation to the structure of the molecule. Biochemistry. 7:208-223.
    • (1968) Biochemistry , vol.7 , pp. 208-223
    • Mihalyi, M.1
  • 48
    • 0025113207 scopus 로고
    • Fibrin polymerization and its regulatory role in hemostasis
    • Mosesson, M. W. 1990. Fibrin polymerization and its regulatory role in hemostasis. J. Lab. Clin. Med. 116:8-17.
    • (1990) J. Lab. Clin. Med. , vol.116 , pp. 8-17
    • Mosesson, M.W.1
  • 49
    • 0027247825 scopus 로고
    • Evidence for a second type of fibril branch point in fibrin polymer networks, the trimolecular junction
    • Mosesson, M. W., J. P. DiOrio, K. R. Siebenlist, J. S. Wall, and J. F. Hainfeld. 1993. Evidence for a second type of fibril branch point in fibrin polymer networks, the trimolecular junction. Blood. 82-1517-1521.
    • (1993) Blood , vol.82 , pp. 1517-1521
    • Mosesson, M.W.1    DiOrio, J.P.2    Siebenlist, K.R.3    Wall, J.S.4    Hainfeld, J.F.5
  • 51
    • 0019779251 scopus 로고
    • Identification and mass analysis of human fibrinogen molecules and their domains by scanning transmission electron microscopy
    • Mosesson, M. W., J. Hainfeld, J. Wall, and R. H. Haschemeyer. 1981. Identification and mass analysis of human fibrinogen molecules and their domains by scanning transmission electron microscopy. J. Mol. Biol. 153:695-718.
    • (1981) J. Mol. Biol. , vol.153 , pp. 695-718
    • Mosesson, M.W.1    Hainfeld, J.2    Wall, J.3    Haschemeyer, R.H.4
  • 52
    • 0029111701 scopus 로고
    • The role of fibrinogen D domain intermolecular association sites in the polymerization of fibrin and fibrinogen Tokyo II (γ275 Arg→Cys)
    • Mosesson, M. W., K. R. Siebenlist, J. P. DiOrio, M. Matsuda, J. F. Hainfeld, and J. S. Wall. 1995. The role of fibrinogen D domain intermolecular association sites in the polymerization of fibrin and fibrinogen Tokyo II (γ275 Arg→Cys). J. Clin. Invest. 96:1053-1058.
    • (1995) J. Clin. Invest. , vol.96 , pp. 1053-1058
    • Mosesson, M.W.1    Siebenlist, K.R.2    DiOrio, J.P.3    Matsuda, M.4    Hainfeld, J.F.5    Wall, J.S.6
  • 53
    • 0018128932 scopus 로고
    • Fibrinogen-fibrin transformations characterized during the course of reaction by their intermediate structures. A light scattering study in dilute solution under physiological, conditions
    • Müller, M., and W. Burchard. 1978. Fibrinogen-fibrin transformations characterized during the course of reaction by their intermediate structures. A light scattering study in dilute solution under physiological, conditions. Biochim. Biophys. Acta. 537:208-225.
    • (1978) Biochim. Biophys. Acta , vol.537 , pp. 208-225
    • Müller, M.1    Burchard, W.2
  • 54
    • 0019455004 scopus 로고
    • Fibrinogen-fibrin transformation. 2. Influence of temperature, pH and of various enzymes on the intermediates
    • Müller, M., H. Lasarcyk, and W. Burchard. 1981. Fibrinogen-fibrin transformation. 2. Influence of temperature, pH and of various enzymes on the intermediates. Int. J. Biol. Macromol. 3:19-24.
    • (1981) Int. J. Biol. Macromol. , vol.3 , pp. 19-24
    • Müller, M.1    Lasarcyk, H.2    Burchard, W.3
  • 55
    • 0019321329 scopus 로고
    • Kinetics of ligation of fibrin oligomers
    • Nelb, G. W., G. W. Kamykowski, and J. D. Ferry. 1980. Kinetics of ligation of fibrin oligomers. J. Biol. Chem. 255:6398-6402.
    • (1980) J. Biol. Chem. , vol.255 , pp. 6398-6402
    • Nelb, G.W.1    Kamykowski, G.W.2    Ferry, J.D.3
  • 57
    • 0001211464 scopus 로고
    • Significance of cryoprofibrin in fibrinogen-fibrin conversion
    • Shainoff, J. R., and I. H. Page. 1962. Significance of cryoprofibrin in fibrinogen-fibrin conversion. J. Exp. Med. 116:687-707.
    • (1962) J. Exp. Med. , vol.116 , pp. 687-707
    • Shainoff, J.R.1    Page, I.H.2
  • 60
    • 0342809110 scopus 로고
    • Oher einige thermodynamische eigen schaften von Fibrinogenlösungen und Gund der lichtstreuungsmethode
    • Schulz, G. V., and H. A. Ende. 1963. Oher einige thermodynamische Eigen schaften von Fibrinogenlösungen und Gund der Lichtstreuungsmethode. Z. Phys. Chem. 36:82-96.
    • (1963) Z. Phys. Chem. , vol.36 , pp. 82-96
    • Schulz, G.V.1    Ende, H.A.2
  • 61
    • 0030848486 scopus 로고    scopus 로고
    • Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin
    • Spraggon, G., S. J. Everse, and R. F. Doolittle. 1997. Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin. Nature. 389:455-462.
    • (1997) Nature , vol.389 , pp. 455-462
    • Spraggon, G.1    Everse, S.J.2    Doolittle, R.F.3
  • 63
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 64
    • 0027379584 scopus 로고
    • Carboxyl-terminal portions of the α-chains of fibrinogen and fibrin. Localization by electron microscopy and the effects of isolated αC fragments on polymerization
    • Veklich, Y. I., O. V. Gorkun, L. V. Medved, W. Nieuwenhuizen, and J. W. Weisel. 1993. Carboxyl-terminal portions of the α-chains of fibrinogen and fibrin. Localization by electron microscopy and the effects of isolated αC fragments on polymerization. J. Biol. Chem. 268: 13577-13585.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13577-13585
    • Veklich, Y.I.1    Gorkun, O.V.2    Medved, L.V.3    Nieuwenhuizen, W.4    Weisel, J.W.5
  • 65
    • 0019972087 scopus 로고
    • On the kinetics of the thrombin-controlled polymerization of fibrin
    • Visser, A., and T. A. Payens. 1982. On the kinetics of the thrombin-controlled polymerization of fibrin. FEBS Lett. 142:35-38.
    • (1982) FEBS Lett. , vol.142 , pp. 35-38
    • Visser, A.1    Payens, T.A.2
  • 66
    • 0022967224 scopus 로고
    • Fibrin assembly. Lateral aggregation and the role of the two pairs of fibrinopeptides
    • Weisel, J. W. 1986. Fibrin assembly. Lateral aggregation and the role of the two pairs of fibrinopeptides. Biophys. J. 50:1079-1093.
    • (1986) Biophys. J. , vol.50 , pp. 1079-1093
    • Weisel, J.W.1
  • 67
    • 0026771894 scopus 로고
    • Computer modeling of fibrin polymerization kinetics correlated with electron microscope and turbidity observations: Clot structure and assembly are kinetically controlled
    • Weisel, J. W., and C. Nagaswami. 1992. Computer modeling of fibrin polymerization kinetics correlated with electron microscope and turbidity observations: clot structure and assembly are kinetically controlled. Biophys. J. 63:111-128.
    • (1992) Biophys. J. , vol.63 , pp. 111-128
    • Weisel, J.W.1    Nagaswami, C.2
  • 68
  • 69
    • 0027194661 scopus 로고
    • The sequence of cleavage of fibrinopeptides from fibrinogen is important for protofibril formation and enhancement of lateral aggregation in fibrin clots
    • Weisel, J. W., Y. Veklich, and O. Gorkun. 1993. The sequence of cleavage of fibrinopeptides from fibrinogen is important for protofibril formation and enhancement of lateral aggregation in fibrin clots. J. Mol. Biol. 232:285-297.
    • (1993) J. Mol. Biol. , vol.232 , pp. 285-297
    • Weisel, J.W.1    Veklich, Y.2    Gorkun, O.3
  • 71
    • 0020379343 scopus 로고
    • Fibrin polymerization studied by elastic and dynamic light-scattering as a function of fibrinopeptide A release
    • Wiltzius, P., G. Dietler, W. Känzig, A. Häberli, and P. W. Straub. 1982b. Fibrin polymerization studied by elastic and dynamic light-scattering as a function of fibrinopeptide A release. Biopolymers. 21:2205-2223.
    • (1982) Biopolymers , vol.21 , pp. 2205-2223
    • Wiltzius, P.1    Dietler, G.2    Känzig, W.3    Häberli, A.4    Straub, P.W.5
  • 72
    • 85031597337 scopus 로고    scopus 로고
    • Wyatt Technology Corporation, Santa Barbara, CA
    • Wyatt Technology Corporation. 1997. ASTRA Manual 4.50. Wyatt Technology Corporation, Santa Barbara, CA.
    • (1997) ASTRA Manual 4.50
  • 73
    • 0016104414 scopus 로고
    • Light scattering from wormlike chains. Determination of the shift factor
    • Yamakawa, H., and M. Fujii. 1974. Light scattering from wormlike chains. Determination of the shift factor. Macromolecules. 7:649-654.
    • (1974) Macromolecules , vol.7 , pp. 649-654
    • Yamakawa, H.1    Fujii, M.2
  • 74
    • 5844368173 scopus 로고
    • The scattering of light and the radial distribution functions of high polymer solutions
    • Zimm, B. H. 1948. The scattering of light and the radial distribution functions of high polymer solutions. J. Chem. Phys. 16:1093-1116.
    • (1948) J. Chem. Phys. , vol.16 , pp. 1093-1116
    • Zimm, B.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.