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THE EVOLUTIONARY RELATIONSHIPS OF THE ENZYMES INVOLVED IN BLOOD COAGULATION AND HEMOSTASIS *

dc.contributor.authorHewett-Emmett, Daviden_US
dc.contributor.authorCzelusniak, Johnen_US
dc.contributor.authorGoodman, Morrisen_US
dc.date.accessioned2010-06-01T20:30:36Z
dc.date.available2010-06-01T20:30:36Z
dc.date.issued1981-06en_US
dc.identifier.citationHewett-Emmett, David; Czelusniak, John; Goodman, Morris (1981). "THE EVOLUTIONARY RELATIONSHIPS OF THE ENZYMES INVOLVED IN BLOOD COAGULATION AND HEMOSTASIS * ." Annals of the New York Academy of Sciences 370(1): 511-527. <http://hdl.handle.net/2027.42/73621>en_US
dc.identifier.issn0077-8923en_US
dc.identifier.issn1749-6632en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/73621
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6455952&dopt=citationen_US
dc.format.extent798710 bytes
dc.format.extent3109 bytes
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dc.publisherBlackwell Publishing Ltden_US
dc.rights1981 The New York Academy of Sciencesen_US
dc.titleTHE EVOLUTIONARY RELATIONSHIPS OF THE ENZYMES INVOLVED IN BLOOD COAGULATION AND HEMOSTASIS *en_US
dc.typeArticleen_US
dc.subject.hlbsecondlevelScience (General)en_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Human Genetics University of Michigan Medical School Ann Arbor, Michigan 48109en_US
dc.contributor.affiliationumDepartment of Anatomy Wayne State University School of Medicine Detroit, Michigan 48201en_US
dc.identifier.pmid6455952en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/73621/1/j.1749-6632.1981.tb29759.x.pdf
dc.identifier.doi10.1111/j.1749-6632.1981.tb29759.xen_US
dc.identifier.sourceAnnals of the New York Academy of Sciencesen_US
dc.identifier.citedreferenceSeegers, W. H., H. I. Hassouna, D. Hewett-Emmett, D. A. Walz & T. J. Andary. 1975. Prothrombin and thrombin. Selected aspects of thrombin formation, properties, inhibition and immunology. Sem. Thrornb. Hemost. 1: 211 – 283.en_US
dc.identifier.citedreferenceDavie, E. W. & K. Fujikawa. 1975. Basic mechanisms in blood coagulation. Ann. Rev. Biochem. 44: 799 – 829.en_US
dc.identifier.citedreferenceSuttie, J. W. & C. M. Jackson. 1977. Prothrombin structure, activation and biosynthesis. Physiol. Rev. 57: 1 – 70.en_US
dc.identifier.citedreferenceTsernoglou, D., D. A. Wlaz, L. E. McCoy & W. H. Seegers. 1974. An X-ray crystallographic study of thrombin. J. Biol. Chem. 249: 999.en_US
dc.identifier.citedreferenceSegal, D. M., J. C. Powers, G. H. Cohen, D. R. Davies & P. E. Wilcox. 1971. Substrate binding site in chymotrypsin A Γ. Biochemistry 10: 3728 – 3738.en_US
dc.identifier.citedreferenceStuoud, R. M. 1974. A family of protein-cutting proteins. Sci. Am. 231: 74 – 88.en_US
dc.identifier.citedreferenceDe HaËn, C., H. Neurath & D. C. Teller. 1975. The phylogeny of trypsinrelated serine proteases and their zymogens. New methods for the investigation of distant evolutionary relationships. J. Mol. Biol. 92: 225 – 259.en_US
dc.identifier.citedreferenceYoung, C. L., W. C. Barker, C. M. Tomaselli & M. O. Dayhoff. 1978. Serine proteases. In Atlas of Protein Sequence and Structure. M. O. Dayhoff, Ed. Vol. 5 ( Suppl. 3 ): 73 – 89. National Biomedical Research Foundation. Washington, D.C.en_US
dc.identifier.citedreferenceKurosky, A., D. R. Barnett, T.-H. Lee, B. Touchstone, R. E. Hay, M. S. Arnott, B. H. Bowman & W. M. Fitch. 1980. Covalent structure of human haptoglobin: A serine protease homolog. Proc. Natl. Acad. Sci. USA 77: 3388 – 3392.en_US
dc.identifier.citedreferenceGoodman, M., I. Czelusniak, G. W. Moore, A. E. Romero-Herrera & G. Matsuda. 1979. Fitting the gene linkage into its species linkage, a parsimony strategy illustrated by cladograms constructed from globin sequences. Syst. Zool. 28: 132 – 163.en_US
dc.identifier.citedreferenceGoodman, M., J.-F. PechÈre, J. Haiech & J. G. Demaille. 1979. Evolutionary diversification of structure and function in the family of intracellular calcium-binding proteins. I. Mol. Evol. 13: 331 – 352.en_US
dc.identifier.citedreferenceTashian, R. E., D. Hewett-Emmett & M. Goodman. Evolutionary diversity in the structure and activity of carbonic anhydrase. In Protides of the Biological Fluids. Colloquium No. 28. H. Peeters, Ed.: 153 – 156. Pergamon Press. Oxford.en_US
dc.identifier.citedreferenceMoore, G. W. & M. Goodman. 1977. Alignment statistic for identifying related protein sequences. J. Mol. Evol. 9: 121 – 130.en_US
dc.identifier.citedreferenceWalz, D. A., D. Hewett-Emmett & W. H. Seegers. 1977. Amino acid sequence of human prothrombin fragments 1 and 2. Proc. Natl. Acad. Sci. USA 74: 1969 – 1972.en_US
dc.identifier.citedreferenceButkowski, R. J., J. Elion, M. R. Downing & K. G. Mann. 1977. Primary structure of human prethrombin 2 and Α-thrombin. I. Biol. Chem. 252: 4942 – 4957.en_US
dc.identifier.citedreferenceThompson, A. R., D. L. Enfield, L. H. Ericsson, M. E. Legaz & J. W. Fenton II. 1977. Human thrombin: Partial primary structure. Arch. Biochem. Biophys. 178: 356 – 367.en_US
dc.identifier.citedreferenceReuterby, J., D. A. Walz, L. E. McCoy & W. H. Seegers. 1974. Amino acid sequence of O fragment of bovině prothrombin. Thromb. Res. 4: 885 – 890.en_US
dc.identifier.citedreferenceHewett-Emmett, D., L. E. McCoy, H. I. Hassouna, J. Reuterby, D. A. Walz & W. H. Seegers. 1974. A partial gene duplication in the evolution of prothrombin ? Thromb. Rcs. 5: 421 – 430.en_US
dc.identifier.citedreferenceHewett-Emmett, D., D. A. Walz, J. Reuterby, L. E. McCoy & W. H. Seegers. 1975. The amino acid sequence of PR fragment (NH 2 -terminal fragment) of bovine prothrombin. Thromb. Res. 7: 227 – 234.en_US
dc.identifier.citedreferenceMagnusson, S., T. E. Petersen, L. Sottrup-Jensen & H. Claeys. 1975. Complete primary structure of prothrombin. In Proteases and Biological Control. E. Reich, D. B. Rifkin & E. Shaw, Eds.: 123 – 149. Cold Spring Harbor Laboratory. Cold Spring Harbor, N. Y.en_US
dc.identifier.citedreferenceWalz, D. A. 1978. Comparative aspects of prothrombin activation. Bibliotheca Haemat. 44: 8 – 14.en_US
dc.identifier.citedreferenceTitani, K., K. Fujikawa, D. L. Enfield, L. H. Ericsson, K. A. Walsh & H. Neurath. 1975. Bovine factor X (Stuart factor): Amino acid sequence of heavy chain. Proc. Natl. Acad. Sci. USA 72: 3082 – 3086.en_US
dc.identifier.citedreferenceEnfield, D. L., L. H. Ericsson, K. Fujikawa, K. A. Walsh, H. Neurath & K. Titani. 1979. Amino acid sequence of the light chain of bovine factor X, (Stuart factor). Biochemistry 19: 659 – 667.en_US
dc.identifier.citedreferenceKatayama, K., L. H. Ericsson, D. L. Enfield, K. A. Walsh, H. Neurath E. W. Davie & K. Titani. 1979. Comparison of amino acid sequence of bovine coagulation factor IX (Christmas factor) with that of other vitamin K-dependent plasma proteins. Proc. Natl. Acad. Sci. USA 76: 4990 – 4994.en_US
dc.identifier.citedreferenceFernlund, P. & J. Stenflo. 1980. Amino acid sequence of bovine protein C. In Vitamin K Metabolism and Vitamin K-dependent Proteins. J. W. Suttie, Ed.: 84 – 88. University Park Press. Baltimore, Md.en_US
dc.identifier.citedreferenceKisiel, W., K. Fujikawa & E. W. Davie. 1977. Activation of bovine factor VII (proconvertin) by factor XIIa (activated Hageman factor). Biochemistry 16: 4189 – 4194.en_US
dc.identifier.citedreferenceDiscipio, R. G. & E. W. Davie. 1979. Characterization of protein S, a Γ-carboxyglutamic acid containing protein from bovine and human plasma. Biochemistry 18: 899 – 904.en_US
dc.identifier.citedreferenceKoide, T., M. A. Hermodson & E. W. Davie. 1977. Active site of bovine factor XI (plasma thromboplastin antecedent). Nature 266: 729 – 730.en_US
dc.identifier.citedreferenceKurachi, K. & E. W. Davie. 1977. Activation of human factor XI (plasma thromboplastin antecedent) by factor XIIa (activated Hageman factor). Biochemistry 16: 5831 – 5839.en_US
dc.identifier.citedreferenceFujikawa, K., K. Kurachi & E. W. Davie. 1977. Characterization of bovine factor XIIa (activated Hageman factor). Biochemistry 16: 4182 – 4188.en_US
dc.identifier.citedreferenceWiman, B. 1977. Primary structure of the Β-chain of human plasmin. Eur. J. Biochem. 76: 129 – 137.en_US
dc.identifier.citedreferenceSottrup-Jensen, L., H. Claeys, M. Zajdel, T. E. Petersen & S. Magnusson. 1978. The primary structure of human plasmhogen isolation of two lysine-binding fragments and one “mini”-plasminogen (MW, 38,000) by elastase-catalysed-specific limited proteolysis. In Progress in Chemical Fibrinolysis and Thrombolysis. J. F. Davidson, R. M. Rowan, M. M. Samama & P. C. Desnogens, Eds. Vol. 3: 191 – 209. Raven Press. New York.en_US
dc.identifier.citedreferenceKurosky, A., D. R. Barnett, M. A. Rasco, T.-H. Lee & B. H. Bowman. 1974. Evidence of homology between the Β-chain of human haptoglobin and the chymotrypsin family of serine proteases. Biochem. Genet. 11: 279 – 293.en_US
dc.identifier.citedreferenceKurosky, A., H.-H. Kim & B. Touchstone. 1976. Comparative sequence analysis of the N-terminal region of rat, rabbit and dog haptoglobin Β-chains. Comp. Biochem. Physiol. 55: 453459.en_US
dc.identifier.citedreferenceTschesche, H., G. Mair, G. Godec, F. Fiedler, W. Ehret, C. Hirschauer, M. Lemon & H. Fritz. 1979. The primary structure of porcine glandular kallikrein. Adv. Exp. Med. & Biol. 120: 245 – 260.en_US
dc.identifier.citedreferenceDayhoff, M. O. 1972. Proteases related to trypsin. In Atlas of Protein Sequence and Structure. M. O. Dayhoff, Ed. Vol. 5: D99 – D111. National Biomedical Research Foundation. Washington, D.C.en_US
dc.identifier.citedreferenceKramer, K. J., R. L. Felsted & J. H. Law. 1973. Cocoonase. V. Structural studies on an insect serine protease. J. Biol. Chem. 248: 3021 – 3028.en_US
dc.identifier.citedreferenceKisiel, W. 1979. Molecular properties of the factor V-activating enzyme from Russell'sviper venom. I. Biol. Chem. 254: 12230 – 12234.en_US
dc.identifier.citedreferenceBaumgartner, R., T. Fletcher, I. Theodor, S. S. Bajwa, F. S. Markland & H. Pirkle. 1980. Amino acid sequences in crotolase, a thrombin-like enzyme from the venom of Crotalus adamanteus. Fed. Proc. 39: 1027 (Abst # 4001).en_US
dc.identifier.citedreferenceSim, R. B., R. R. Porter, K. B. M. Reid & I. Gigli. 1977. The structure and enzymatic activities of the C1r and C1s subcomponents of C1, the first component of human serum complement. Biochem. J. 163: 219 – 227.en_US
dc.identifier.citedreferenceVolanakis, J. E., A. S. Bhown, J. C. Bennett & J. E. Mole. 1980. Partial amino acid sequence of human factor D: Homology with serine proteases. Proc. Natl. Acad. Sci. USA 77: 1116 – 1119.en_US
dc.identifier.citedreferenceWoodbury, R. G., N. Katunuma, K. Kobayashi, K. Titani & H. Neurath. 1978. Covalent structure of a group-specific protease from rat small intestine. Biochemistry 17: 811 – 819.en_US
dc.identifier.citedreferenceOlafson, R. W., L. JurÁsek, M. R. Carpenter & L. B. Smillie. 1975. Amino acid sequence of Streptomyces griseus trypsin. Biochemistry 14: 1168 – 1177.en_US
dc.identifier.citedreferenceCook, C. N. & D. Hewett-Emmett. 1974. The uses of protein sequence data in systematics. In Prosirnian Biology. R. D. Martin, G. A. Doyle & A. C. Walker, Eds.: 937 – 958. Duckworth. London.en_US
dc.identifier.citedreferenceHartley, B. S. 1970. Homologies in serine proteinases. Phil. Trans. Royal Soc. London B 257: 77 – 81.en_US
dc.identifier.citedreferenceHartley, B. S. 1979. Evolution of enzyme structure. Proc. Royal Soc. London B 205: 443 – 452.en_US
dc.identifier.citedreferenceJohnson, P. & L. B. Smillie. 1974. The amino acid sequence and predicted structure of Streptomyces griseus protease B. FEBS Lett. 47: 1 – 6.en_US
dc.identifier.citedreferenceFitch, W. M. 1977. Phylogenies constrained by the crossover process as illustrated by human hemoglobins and a thirteen-cycle, eleven-amino-acid repeat in human apolipoprotein A-1. Genetics 86: 632 – 644.en_US
dc.identifier.citedreferenceHewett-Emmett, D., D. A. Walz & W. H. Seegers. 1977. Evolutionary and functional observations on the primary structure of the non-thrombin region (residues 1–273) of human prothrombin. Biochem. Soc. Trans. (UK) 5: 1452 – 1455.en_US
dc.identifier.citedreferenceHwett-Emmett, D. 1978. Amino acid sequence homology and the vitamin K-dependent proteins. Bibliotheca Haemat. 44: 94 – 104.en_US
dc.identifier.citedreferenceDoolittle, R. F. 1979. 3rd Edit. Protein evolution. In The Proteins. H. Neurath & R. L. Hill, Eds.: 1 – 118. Academic Press, Inc. New York.en_US
dc.identifier.citedreferenceBradshaw, R. A., G. A. Grant, K. A. Thomas & A. Z. Eisen. 1980. Mouse NGF Γ subunit and crab collagenase: Two serine proteases of unusual function. In Protides of the Biological Fluids. Colloquium No. 28. H. Peeters, Ed.: 119 – 122. Pergamon Press. Oxford.en_US
dc.identifier.citedreferenceBrunisholz, R., P. Moser, J. Schaller & E. Rickli. 1980. Partial sequence comparison between human, bovine and porcine plasrninogen. In Protides of the Biological Fluids. Colloquium No. 28. H. Peeters, Ed.: 103 – 106. Pergamon Press. Oxford.en_US
dc.identifier.citedreferenceMole, J. E. & M. Niemann. 1980. Structural evidence that complement factor B constitutes a novel class of serine protease. J. Biol. Chem. 255: 8472 – 8476.en_US
dc.identifier.citedreferenceWoodbury, R. G. & H. Neurath. 1980. Structure, specificity and localization of the serine proteases of connective tissue. FEBS Lett. 114: 189 – 196.en_US
dc.identifier.citedreferencePetersen, T. E., H. C. ThØersen, L. Sottrup-Jensen, S. Magnusson & H. Jornvall. 1980. Isolation and N -terminal sequence of protein Z, a Γ-car-boxyglutamic acid containing protein from bovine plasma. FEBS Lett. 114: 278 – 282.en_US
dc.identifier.citedreferenceProwse, C. W. & M. P. Esnouf. 1977. The isolation of a new warfarin-sensitive protein from bovine plasma. Biochem. Soc. Trans. (UK) 5: 255 – 256.en_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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