Multiple forms of medicinal leech destabilase-lysozyme

Biochemical and Biophysical Research Communications

Volumn 306, Issue 1, 2003, Pages 318-323

  Zavalova, L L ^a   Artamonova, I I ^a   Berezhnoy, S N ^a   Tagaev, A A ^a   Baskova, I P ^b   Andersen, J ^c   Roepstorff, P ^c   Egorov, Ts A ^a  

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

^b MOSCOW STATE UNIVERSITY   (Russian Federation)

^c UNIVERSITY OF SOUTHERN DENMARK   (Denmark)

Author keywords

Destabilase lysozyme; Enzyme isoforms; Mass spectrometry

Indexed keywords

DESTABILASE LYSOZYME; HIRUDIN; LYSOZYME; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; CORRELATION ANALYSIS; ENZYME ANALYSIS; ENZYME ISOLATION; GENETIC CODE; GENETIC HETEROGENEITY; LEECH; MASS SPECTROMETRY; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; PROTEIN FAMILY; WILD TYPE;

GENETTA; HIRUDINIDA; HIRUDO MEDICINALIS;

EID: 0037716474     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(03)00896-9     Document Type: Article

References (10)

1. Zavalova L.L., Baskova I.P., Lukyanov S.A., Sass A.V., Snezhkov E.V., Akopov S.A., Artamonova I.I., Archipova V.S., Nesmeyanov V.A., Kozlov D.G., Benevolensky S.V., Kiseleva V.I., Poverenny A.M., Sverdlov E.D. Destabilase from the medicinal leech is a representative of a novel family of lysozymes. Biochim. Biophys. Acta. 1478:2000;69-77.
2. 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 to dissolve blood clots. Mol. Gen. Genet. 253:1996;20-25.
3. Fradkov A., Berezhnoy S., Barsova E., Zavalova L., Lukyanov S., Baskova I., Sverdlov E. Enzyme from the medicinal leech (Hirudo medicinalis) that specifically splits ε(γ-Glu)-Lys isopeptide bonds: cDNA coding and protein structure. FEBS Lett. 390:1996;145-148.
4. Nilsen I.W., Myrnes B. The gene of chlamisine, a marine invertebrate-type lysozyme, is organized similar to vertebrate but different from invertebrate chicken-type lysozyme gene. Gene. 269:2001;27-32.
5. 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.
6. Bachali S., Jager M., Hassanin A., Schoentgen F., Jolles P., Fiala-Medioni A., Deutsch J.S. Phylogenetic analysis of the invertebrate lysozymes and the evolution of lysozyme function. J. Mol. Evol. 54:2002;652-664.
7. Friedman M., Krull L.H., Cavins J. The chromatographic determination of cystine and cysteine residues in proteins as S-β-(4-pyridylethyl)cysteine. J. Biol. Chem. 245:1970;3868-3871.
8. Gross E., Witkop B. Selective cleavage of the methionyl peptide bonds in ribonuclease with cyanogen bromide. J. Am. Chem. Soc. 83:1961;1510-1511.
9. Houmard J., Drapeau G.R. Staphylococcal protease: a proteolytic enzyme specific for glutamyl bonds. Proc. Natl. Acad. Sci. USA. 69:1972;3506-3509.
10. Sawyer R.T. Leech Biology and Behaviour. 1986;Oxford University Press, Oxford.