Purification and some properties of streptococcal NAD-glycohydrolase

FEMS Microbiology Letters

Volumn 136, Issue 1, 1996, Pages 71-78

  Gerlach, D ^a   Ozegowski, J H ^a   Gunther E ^a   Vettermann, S ^b   Kohler W ^a  

^a FRIEDRICH SCHILLER UNIVERSITY JENA   (Germany)

^b FRITZ LIPMANN INSTITUTE   (Germany)

Author keywords

NAD glycohydrolase; Streptococcal protease; Streptodornase

Indexed keywords

NICOTINAMIDE ADENINE DINUCLEOTIDE NUCLEOSIDASE; PROTEINASE; STREPTODORNASE;

AMINO ACID SEQUENCE; ARTICLE; ENZYME ACTIVITY; ENZYME ISOLATION; ENZYME PURIFICATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; STREPTOCOCCUS GROUP C;

STREPTOCOCCUS SP. 'GROUP C';

EID: 0030020604     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/0378-1097(95)00495-5     Document Type: Article

References (22)

1. Alivisatos, S.G.A. (1959) Mechanism of action of nucleotidases. Nature 183, 1034-1037.
2. Ayoub, E.M. and Ferretti, J.J. (1966) Use of bisulfite in the streptococcal anti-nicotinamide adenine dinucleotidase test. Appl. Microbiol. 14, 391-393.
3. Bernheimer, A.W., Lazarides, P.D. and Wilson, A.T. (1957) Diphosphopyridine nucleotidase as an extracellular product of streptococcal growth and its possible relationship to leucotoxicity. J. Exp. Med. 106, 27-37.
4. Brömme, D. and Fittkau, S. (1985) A new substrate and two inhibitors applicable for thermitase, subtilisin BPN′ and α-chymotrypsin. Comparison of kinetic parameters with customary substrates and inhibitors. Biomed. Biochim. Acta 44, 1089-1094.
5. Carlson, A.S., Kellner, A. and Bernheimer, A.W. (1956) Selective inhibition by preparations of streptococcal culture filtrates of the oxidative metabolism of mitochondria procured from rabbit myocardium. J. Exp. Med. 104, 577-587.
6. Carlson, A.S., Kellner, A., Bernheimer, A.W. and Freeman, E.B. (1957) A streptococcal enzyme that acts specifically upon diphosphopyridine nucleotide: characterization of the enzyme and its separation from streptolysin O. J. Exp. Med. 106, 15-26.
7. Christensen, L.R. (1949) Methods for measuring the activity of components of the streptococcal fibrinolytic system, and streptococcal deoxyribonuclease. J. Clin. Invest. 28, 163-172.
8. Everse, K.E., Everse, J. and Simeral, L.S. (1980) B. subtilis NADase and its specific protein inhibitor. Methods Enzymol. 66, 137-144.
9. + glycohydrolase in serum. Clin. Chem. 39, 1007-1011.
10. Gerlach, D., Köhler, W., Günther, E. and Mann, K. (1993) Purification and characterization of streptolysin O secreted by Streptococcus equisimilis (group C). Infect. Immun. 61, 2727-2731.
11. Holm, S.E. and Kaijser (1967) An intracellular inhibitor of streptococcal DPNase in beta-hemolytic streptococci. Acta Pathol. Microbiol. Scand. 69, 277-286.
12. +-glycohydrolase from Streptococcus pyogenes shows cyclic ADP-ribose forming activity. FEMS Microbiol. Lett. 130, 201-204.
13. Kim, U.H., Han, M.K., Bark, B.H. and Kim, H.R. (1993) Purification and characterization of NAD glycohydrolase from rabbit erythrocytes. Arch. Biochem. Biophys. 305, 147-152.
14. Knöll, H., Šramek, J., Vrbová, K., Gerlach, D., Reichardt, W. and Köhler, W. (1991) Scarlet fever and types of erythrogenic toxins produced by the infecting streptococcal strains. Zbl. Bakt. 276, 94-106.
15. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 224, 381-385.
16. Louvard, D., Maroux, S., Vannier, C. and Desnuelle, P. (1975) Topological studies on the hydrolases bound to the intestinal brush border membrane. I. Solubilization by papain and Triton X-100. Biochem. Biophys. Acta 375, 236-248.
17. Ozegowski, J.-H. and Gerlach, D. (1982) Ein empfindlicher Nachweis proteolytischer Aktivität in Kulturfiltraten. Zbl. Bakt. Hyg. A254, 229-233.
18. Pace, M., Agnellini, D., Lippoli, G., Pietta, P.G., Mauri, P.L. and Cinquanta, S. (1991) Purification of NAD glycohydrolase from Neurospora crassa conidia by a polyclonal immunoadsorbent. J. Chromatogr. 539, 517-523.
19. Smyth, C.J. and Fehrenbach, F.J. (1974) Isoelectric analysis of haemolysins and enzymes from streptococci of groups A, C, and G. Acta Pathol. Microbiol. Scand. B 82, 860-870.
20. Winter, J.E. and Bernheimer, A.W. (1961) The deoxyribonucleases of Streptococcus pyogenes. J. Biol. Chem. 239, 215-221.
21. Wolinowska, R., Ceglowski, P., Kok, J. and Venema, G. (1991) Isolation, sequence and expression in Escherichia coli, Bacillus subtilis and Lactococcus lactis of the DNase (Streptodornase)-encoding gene from Streptococcus equisimilis H46A. Gene 106, 115-119.
22. Zahradnïk, F.J. (1977) Streptococcal extracellular NAD-glycohydrolase. Optimal temperature and activation by cysteine. Folia Microbiol. 22, 92-97.