Destabilase from the medicinal leech is a representative of a novel family of lysozymes

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1478, Issue 1, 2000, Pages 69-77

  Zavalova, L L ^a   Baskova, I P ^b   Lukyanov, S A ^a   Sass, A V ^a   Snezhkov, E V ^a   Akopov, S B ^a   Artamonova, I I ^a   Archipova, V S ^a   Nesmeyanov, V A ^a   Kozlov, D G ^c   Benevolensky, S V ^c   Kiseleva, V I ^d   Poverenny, A M ^d   Sverdlov, E D ^a  

^a SHEMYAKIN OVCHINNIKOV INSTITUTE OF BIOORGANIC CHEMISTRY   (Russian Federation)

^b MOSCOW STATE UNIVERSITY   (Russian Federation)

^c STATE RESEARCH INSTITUTE OF GENETICS AND SELECTION OF INDUSTRIAL MICROORGANISMS   (Russian Federation)

^d INSTITUTE OF BIOMEDICAL CHEMISTRY   (Russian Federation)

Author keywords

Antibodies to destabilase; Baculovirus expression; Destabilase gene family; Lysozyme activity; Medicinal leech

Indexed keywords

DESTABILASE; LYSOZYME; UNCLASSIFIED DRUG; VIRUS VECTOR;

ANTIGEN BINDING; ARTICLE; BACULOVIRUS; CAENORHABDITIS ELEGANS; CELL CULTURE; ENZYME ACTIVITY; ENZYME PURIFICATION; ENZYME SPECIFICITY; ESCHERICHIA COLI; EVOLUTION; IMMUNOBLOTTING; IN VITRO STUDY; INSECT; LEECH; MULTIGENE FAMILY; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FAMILY; SEQUENCE HOMOLOGY; YEAST;

AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES; BACULOVIRIDAE; CARBON-NITROGEN LYASES; CELL LINE; DNA, COMPLEMENTARY; ENDOPEPTIDASES; ESCHERICHIA COLI; GENE EXPRESSION; ISOENZYMES; LEECHES; MOLECULAR SEQUENCE DATA; MURAMIDASE; SACCHAROMYCES CEREVISIAE; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY;

BIVALVIA; CAENORHABDITIS ELEGANS; HIRUDINIDA; HIRUDO MEDICINALIS; INSECTA; INVERTEBRATA; MOLLUSCA; UNIDENTIFIED BACULOVIRUS;

EID: 0034673696     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(00)00006-6     Document Type: Article

References (20)

1. Baskova I.P., Nikonov G.I. Destabilase - an enzyme of medicinal leech salivary gland secretion that hydrolyses isopeptide bonds in stabilized fibrin. Biokhimia (USSR). 50:1985;363-375.
2. Zavalova L.L., Kuzina E.V., Levina N.B., Baskova I.P. Monomerization of fragment D-D by destabilase from the medicinal leech does not alter the N-terminal sequence of γ-chain. Thromb. Res. 71:1993;241-244.
3. Zavalova L., Lukyanov S., Baskova I., Snezhkov E., Akopov S., Berezhnoy S., Bogdanova E., Barsova E., Sverdlov E. Genes from the medicinal leech (Hirudo medicinalis) coding for unusual enzymes that specially cleave endo-ε(γ-Glu)-Lys isopeptide bonds and help dissolve blood clots. Mol. Gen. Genet. 253:1996;20-25.
4. Fradkov A., Berezhnoy S., Barsova E., Zavalova L., Lukyanov S., Baskova I., Sverdlov E. Enzyme from the medicinal leech (Hirudo medicinalis) that specifically splits endo-ε(γ-Glu)-Lys isopeptide bonds: cDNA cloning and protein primary structure. FEBS Lett. 390:1996;145-148.
5. Protein Identification Resorce, release, 41, 1994.
6. Jolles J., Jolles P. The lysozyme from Asterias rubens. Eur. J. Biochem. 54:1975;19-23.
7. Jolles P., Charlemagne D., Petit J.F., Maire A.C., Jolles J. Biochimie Comparee des lysozymes. Bull. Soc. Chim. Biol. 47:1965;2241-2259.
8. DNA cloning, volume 111, A practical approach, D.M. Glover (Ed.), IRL Press, Oxford.
9. Kartasheva N.N., Kuchkin S.V., Benevolensky S.V. Genetic aspects of carbon catabolite repression of the STA2 glucoamylase gene in S. cerevisiae. Yeast. 12:1996;1297-1300.
10. Lohr D., Venkov P., Zlatanova J. Transcriptional regulation in the yeast Gal gene family: a complex genetic network. FASEB J. 9:1995;777-787.
11. J. Sambrook, F.F. Fritsch, T. Maniatis, Molecular cloning: a laboratory manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, 1989.
12. Livingstone C., Jones J. Baculovirus expression vectors with single strand capability. Nucleic Acids Res. 17:1989;2366-2367.
13. Matsuura Y., Possee R.D., Overton H.A., Bishop D.H.L. Baculovirus expression vectors: the requirements for high level expression of proteins, including glycoproteins. J. Gen. Virol. 68:1987;1233-1250.
14. Laemmly U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227 N5259:1970;680-685.
15. Antibodies. A laboratory manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, 1988, pp. 479-511.
16. Sedmak J.J., Grossberg S.E. A rapid sensitive and versatile assay for protein using coomassie brilliant. Anal. Biochem. 79:1977;544-552.
17. M. Dixon, E.C. Webb, Enzymes, Longman Group, 1979.
18. Protein data bank, FASTA, GEBBANK: locus CELC45G7, 1987.
19. Jolles J., Fiala-Medioni A., Jolles P. The ruminant digestion model using bacteria already employed early in evolution by symbiotic molluscs. J. Mol. Evol. 43:1996;523-527.
20. Ito Y., Yoshikawa A., Hotani T., Fukuda S., Sugimura K., Imoto T. Amino acid sequences of lysozymes newly purified from invertebrates imply wide distribution of a novel class in the lysozyme family. Eur. J. Biochem. 259:1999;456-461.