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. 1973 May;7(5):731–734. doi: 10.1128/iai.7.5.731-734.1973

Physical Separation of Streptococcal Nicotinamide Adenine Dinucleotide Glycohydrolase from Streptolysin O

S Shany 1, Phyllis S Grushoff 1, Alan W Bernheimer 1
PMCID: PMC422752  PMID: 4357989

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.

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Selected References

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

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