Physical separation of streptococcal nicotinamide adenine dinucleotide glycohydrolase from streptolysin O.

Infection and immunity ·Vol. 7 ·No. 5 ·1973-05-00 ·Pages 731-4

Shany S, Grushoff PS, Bernheimer AW

Abstract

Streptococcal nicotinamide adenine dinucleotide glycohydrolase (NADase) with a molecular weight of about 55,000 and an isoelectric pH of 8.55 was isolated from crude streptolysin O (SLO) preparations. NADase differed from SLO in size, charge, and immunological behavior. Streptococcal NADase is considered to have no role in the hemolytic process because it has no hemolytic activity; conversely, partially purified SLO showed no NADase activity. The hemolytic activity of crude SLO was completely inhibited by anti-tetanolysin, whereas the NADase activity in the same reaction mixture was unaffected. Experiments involving double diffusion in agar also demonstrated immunological nonidentity of the two proteins.

MeSH Terms

Bacteriological Techniques Chromatography, Gel Chromatography, Ion Exchange Electrophoresis, Polyacrylamide Gel Hemolysis Immunodiffusion Isoelectric Focusing Molecular Weight N-Glycosyl Hydrolases/isolation & purification NAD Neutralization Tests Sodium Dodecyl Sulfate Streptococcus pyogenes/enzymology Streptolysins/analysis Tetanus Antitoxin

Chemicals

Streptolysins Tetanus Antitoxin NAD Sodium Dodecyl Sulfate N-Glycosyl Hydrolases

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Shany S

Grushoff P S

Bernheimer A W

References (14)

14 references, click to expand

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Article Info

Journal

Infection and immunity

Abbr.

Infect Immun

ISSN

0019-9567

DOI

10.1128/iai.7.5.731-734.1973

Published

1973-05-00

Pages

731-4

Language

English

Region

United States

NLM ID

0246127

PMCID

PMC422752

Subset

External Links

PubMed source DOI: 10.1128/iai.7.5.731-734.1973 PMC Full Text View journal details

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Physical separation of streptococcal nicotinamide adenine dinucleotide glycohydrolase from streptolysin O.

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