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Volumn 253, Issue 1-2, 1996, Pages 20-25

Genes from the medicinal leech (Hirudo medicinalis) coding for unusual enzymes that specifically cleave endo-ε(γ-Glu)-Lys isopeptide bonds and help to dissolve blood clots

Author keywords

Baculovirus expression vector; Destabilase genes; Endo ( Glu) Lys isopeptidase; Medicinal leech; Protein sequence

Indexed keywords

COMPLEMENTARY DNA; ENZYME; ENZYME PRECURSOR; PEPTIDASE; SIGNAL PEPTIDE;

EID: 0029857709     PISSN: 00268925     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004380050291     Document Type: Article
Times cited : (79)

References (25)
  • 1
    • 0028322985 scopus 로고
    • Transglutaminases: Protein cross-linking enzymes in tissues and body fluids
    • Aeschlimann D, Paulsson M (1994) Transglutaminases: protein cross-linking enzymes in tissues and body fluids. Thrombosis Hacmostasis 71:402-415
    • (1994) Thrombosis Hacmostasis , vol.71 , pp. 402-415
    • Aeschlimann, D.1    Paulsson, M.2
  • 2
    • 0011793844 scopus 로고
    • Destabilase an enzyme of medicinal leech salivary gland secretion that hydrolyzes isopeptide bonds in stabilized fibrin
    • Baskova IP, Nikonov GI (1985) Destabilase an enzyme of medicinal leech salivary gland secretion that hydrolyzes isopeptide bonds in stabilized fibrin. Biokhimiya (USSR) 50:363-375
    • (1985) Biokhimiya (USSR) , vol.50 , pp. 363-375
    • Baskova, I.P.1    Nikonov, G.I.2
  • 3
    • 0026102550 scopus 로고
    • Destabilase, the novel ε-(γ-Glu)-Lys isopeptidase with thrombolytic activity
    • Baskova IP, Nikonov GI (1991) Destabilase, the novel ε-(γ-Glu)-Lys isopeptidase with thrombolytic activity. Blood Coag Fibrinol 2:167-172
    • (1991) Blood Coag Fibrinol , vol.2 , pp. 167-172
    • Baskova, I.P.1    Nikonov, G.I.2
  • 4
    • 0025193292 scopus 로고
    • Hydrolysis of isopeptide ε-(γ-Glutamyl)-Lysine by destabilase from the medicinal leech Hirudo medicinalis
    • Baskova IP, Timokhina EA, Nikonov GI, Stepanov VM (1990) Hydrolysis of isopeptide ε-(γ-Glutamyl)-Lysine by destabilase from the medicinal leech Hirudo medicinalis. Biokhimia (USSR) 55:771-775
    • (1990) Biokhimia (USSR) , vol.55 , pp. 771-775
    • Baskova, I.P.1    Timokhina, E.A.2    Nikonov, G.I.3    Stepanov, V.M.4
  • 6
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomezynski P, Sacchi N (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 162:156-159
    • (1987) Anal Biochem , vol.162 , pp. 156-159
    • Chomezynski, P.1    Sacchi, N.2
  • 7
    • 0026453267 scopus 로고
    • Signal peptidases in prokaryotes and eukaryotes: A new protease family
    • Dalbey RE, von Heijne G (1992) Signal peptidases in prokaryotes and eukaryotes: a new protease family. Trends Biochem Sci 17:474-478
    • (1992) Trends Biochem Sci , vol.17 , pp. 474-478
    • Dalbey, R.E.1    Von Heijne, G.2
  • 9
    • 0014939933 scopus 로고
    • The Chromatographic determination of cystine and cysteine residues in proteins as S-β-(4-pyridylethyl)cysteine
    • Friedman M, Krull LH, Cavins J (1970) The Chromatographic determination of cystine and cysteine residues in proteins as S-β-(4-pyridylethyl)cysteine. J. Biol Chem 245:3868-3871
    • (1970) J. Biol Chem , vol.245 , pp. 3868-3871
    • Friedman, M.1    Krull, L.H.2    Cavins, J.3
  • 10
    • 0024212067 scopus 로고
    • Rapid production of full-length cDNA from rare transcripts: Amplification using a single gene-specific oligonucleotide primer
    • Frohman MA, Dush MK, Martin GR (1988) Rapid production of full-length cDNA from rare transcripts: amplification using a single gene-specific oligonucleotide primer. Proc Natl Acad Sci 85:8998-9002
    • (1988) Proc Natl Acad Sci , vol.85 , pp. 8998-9002
    • Frohman, M.A.1    Dush, M.K.2    Martin, G.R.3
  • 11
    • 0001067208 scopus 로고
    • Selective cleavage of the methionyl peptide bonds in ribonuclease with cyanogen bromide
    • Gross E, Witkop B (1961) Selective cleavage of the methionyl peptide bonds in ribonuclease with cyanogen bromide. J Am Chem Soc 83:1510-1511
    • (1961) J Am Chem Soc , vol.83 , pp. 1510-1511
    • Gross, E.1    Witkop, B.2
  • 12
    • 0026911136 scopus 로고
    • Membrane protein insertion into the endoplasmic reticulum another channel tunnel
    • High S (1992) Membrane protein insertion into the endoplasmic reticulum another channel tunnel. Bio Essays 14:535-540
    • (1992) Bio Essays , vol.14 , pp. 535-540
    • High, S.1
  • 13
    • 0016592228 scopus 로고
    • The lysozyme from Asteris rubens
    • Jolles J, Jolles P (1975) The lysozyme from Asteris rubens. Eur J Bioehem 54: 19-23
    • (1975) Eur J Bioehem , vol.54 , pp. 19-23
    • Jolles, J.1    Jolles, P.2
  • 15
    • 0025792297 scopus 로고
    • Structural features in eukaryotic mRNAs that modulate the initiation of translation
    • Kozak M (1991) Structural features in eukaryotic mRNAs that modulate the initiation of translation. J Biol Chem 266: 19867-19870
    • (1991) J Biol Chem , vol.266 , pp. 19867-19870
    • Kozak, M.1
  • 16
    • 0024547154 scopus 로고
    • Baculovirus expression vectors with single strand capability
    • Livingstone C, Jones J (1989) Baculovirus expression vectors with single strand capability. Nucleic Acids Res 17:2366
    • (1989) Nucleic Acids Res , vol.17 , pp. 2366
    • Livingstone, C.1    Jones, J.2
  • 18
    • 0023091932 scopus 로고
    • Baculovirus expression vectors: The requirements for high level expression of proteins, including glycoproteins
    • Matsuura Y, Possee RD, Overton HA, Bishop DHL (1987) Baculovirus expression vectors: the requirements for high level expression of proteins, including glycoproteins. J Gen Virol 68:1233-1250
    • (1987) J Gen Virol , vol.68 , pp. 1233-1250
    • Matsuura, Y.1    Possee, R.D.2    Overton, H.A.3    Bishop, D.H.L.4
  • 19
    • 0023741661 scopus 로고
    • A highly conserved amino-acid sequence in thrombospondin, properdin and in proteins from sporozoites and blood stages of a human malaria parasite
    • Robson KJH, Hall JRS, Jennings MW, Harris TJR, Marsh K, Newbold CI, Tate VE, Weatherall DJ (1988) A highly conserved amino-acid sequence in thrombospondin, properdin and in proteins from sporozoites and blood stages of a human malaria parasite. Nature 335:79-82
    • (1988) Nature , vol.335 , pp. 79-82
    • Robson, K.J.H.1    Hall, J.R.S.2    Jennings, M.W.3    Harris, T.J.R.4    Marsh, K.5    Newbold, C.I.6    Tate, V.E.7    Weatherall, D.J.8
  • 21
    • 0025735355 scopus 로고
    • Immunoelectrophoretic characterizations of the cross-linking of fibrinogen and fibrin by Factor XIIIa and tissue transglutaminase
    • Shainoff JR, Urbanic DA, DiBello PM (1991) Immunoelectrophoretic characterizations of the cross-linking of fibrinogen and fibrin by Factor XIIIa and tissue transglutaminase. J Biol Chem 266:6429-6437
    • (1991) J Biol Chem , vol.266 , pp. 6429-6437
    • Shainoff, J.R.1    Urbanic, D.A.2    DiBello, P.M.3
  • 22
    • 0023371227 scopus 로고
    • DNA sequence analysis with modified bacteriophage T7 DNA polymerase
    • Tabor S, Richardson CC (1987) DNA sequence analysis with modified bacteriophage T7 DNA polymerase. Proc Natl Acad Sci USA 84:4767-4771
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 4767-4771
    • Tabor, S.1    Richardson, C.C.2
  • 23
    • 0020351368 scopus 로고
    • 2-plasmin inhibitor to fibrin catalyzed by activated fibrin-stabilizing factor
    • 2-plasmin inhibitor to fibrin catalyzed by activated fibrin-stabilizing factor. J Biol Chem 257:14767-14772
    • (1982) J Biol Chem , vol.257 , pp. 14767-14772
    • Tamaki, T.1    Aoki, N.2
  • 24
    • 0025986022 scopus 로고
    • The stabilized fibrin fragment D dimer is a substrate for destabilase (γGlutamyl-ε-Lysyl-isopeptidase)
    • Zavalova LL, Nikonov GI, Kuzina EV, Popova GYu, Baskova IP (1991) The stabilized fibrin fragment D dimer is a substrate for destabilase (γGlutamyl-ε-Lysyl-isopeptidase). Biokhimiya (USSR) 56:115-124
    • (1991) Biokhimiya (USSR) , vol.56 , pp. 115-124
    • Zavalova, L.L.1    Nikonov, G.I.2    Kuzina, E.V.3    Popova, G.Yu.4    Baskova, I.P.5
  • 25
    • 0027303651 scopus 로고
    • Monomerization of fragment D-D by destabilase from the medicinal leech does not alter the N-terminal sequence of the γ-chain
    • Zavalova LL, Kuzina EV, Levina NB, Baskova IP (1993) Monomerization of fragment D-D by destabilase from the medicinal leech does not alter the N-terminal sequence of the γ-chain. Thronib Res 71:241-244
    • (1993) Thronib Res , vol.71 , pp. 241-244
    • Zavalova, L.L.1    Kuzina, E.V.2    Levina, N.B.3    Baskova, I.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.