Skip to main content
PMC home page
The Journal of Experimental Medicine logoLink to The Journal of Experimental Medicine
. 1957 Jul 1;106(1):15–26. doi: 10.1084/jem.106.1.15

A STREPTOCOCCAL ENZYME THAT ACTS SPECIFICALLY UPON DIPHOSPHOPYRIDINE NUCLEOTIDE: CHARACTERIZATION OF THE ENZYME AND ITS SEPARATION FROM STREPTOLYSIN O

Arthur S Carlson 1, Aaron Kellner 1, Alan W Bernheimer 1, Elizabeth B Freeman 1
PMCID: PMC2136732  PMID: 13439111

Abstract

All enzyme that destroys DPN has been found in fractionated and highly concentrated streptococcal preparations that also contain streptolysin O. The enzyme—streptococcal DPNase—was shown by electrophoretic separation and by other means to be distinct from streptolysin O. It is non-dialyzable, heat-labile, and has optimal activity in the pH range 7.2 to 7.8. The enzyme has a high degree of specificity for DPN, which it splits at the nicotinamide-ribose linkage.

Full Text

The Full Text of this article is available as a PDF (573.7 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. BEAVEN G. H., HOLIDAY E. R. Ultraviolet absorption spectra of proteins and amino acids. Adv Protein Chem. 1952;7:319–386. doi: 10.1016/s0065-3233(08)60022-4. [DOI] [PubMed] [Google Scholar]
  2. BERNHEIMER A. W., CARLSON A. S., FREEMAN E. B., KELLNER A. Loss of myocardial contractility induced in isolated mammalian hearts by streptolysin O. J Exp Med. 1956 Sep 1;104(3):361–373. doi: 10.1084/jem.104.3.361. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. BERNHEIMER A. W., CARLSON A. S., KELLNER A. Selective inhibition by preparations of streptococcal filtrates of the oxidative metabolism of mitochondria procured from rabbit myocardium. J Exp Med. 1956 Oct 1;104(4):577–587. doi: 10.1084/jem.104.4.577. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. BERNHEIMER A. W., LAZARIDES P. D., WILSON A. T. Diphosphopyridine nucleotidase as an extracellular product of streptococcal growth and its possible relationship to leukotoxicity. J Exp Med. 1957 Jul 1;106(1):27–37. doi: 10.1084/jem.106.1.27. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Bernheimer A. W. PARALLELISM IN THE LETHAL AND HEMOLYTIC ACTIVITY OF THE TOXIN OF CLOSTRIDIUM SEPTICUM. J Exp Med. 1944 Oct 1;80(4):309–320. doi: 10.1084/jem.80.4.309. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. COLOWICK S. P., KAPLAN N. O., CIOTTI M. M. The reaction of pyridine nucleotide with cyanide and its analytical use. J Biol Chem. 1951 Aug;191(2):447–459. [PubMed] [Google Scholar]
  7. HALBERT S. P., SWICK L., SONN C. The use of precipitin analysis in agar for the study of human streptococcal infections. II. Ouchterlony and Oakley technics. J Exp Med. 1955 May 1;101(5):557–576. doi: 10.1084/jem.101.5.557. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. KAPLAN N. O., COLOWICK S. P., NASON A. Neurospora diphosphopyridine nucleotidase. J Biol Chem. 1951 Aug;191(2):473–483. [PubMed] [Google Scholar]
  9. Mann P. J., Quastel J. H. Nicotinamide, cozymase and tissue metabolism. Biochem J. 1941 Apr;35(4):502–517. doi: 10.1042/bj0350502. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. McIlwain H., Rodnight R. Breakdown of cozymase by a system from nervous tissue. Biochem J. 1949;44(4):470–477. doi: 10.1042/bj0440470. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. NASON A., KAPLAN N. O., COLOWICK S. P. Changes in enzymatic constitution in zinc-deficient Neurospora. J Biol Chem. 1951 Jan;188(1):397–406. [PubMed] [Google Scholar]
  12. RACKER E. Crystalline alcohol dehydrogenase from baker's yeast. J Biol Chem. 1950 May;184(1):313–319. [PubMed] [Google Scholar]

Articles from The Journal of Experimental Medicine are provided here courtesy of The Rockefeller University Press

RESOURCES