Physical separation of streptococcal nicotinamide adenine dinucleotide glycohydrolase from streptolysin O.
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.
D001431:Bacteriological Techniques; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006461:Hemolysis; D005779:Immunodiffusion; D007525:Isoelectric Focusing; D008970:Molecular Weight; D009699:N-Glycosyl Hydrolases / Q000302:isolation & purification*; D009243:NAD; D009500:Neutralization Tests; D012967:Sodium Dodecyl Sulfate; D013297:Streptococcus pyogenes / Q000201:enzymology*; D013301:Streptolysins / Q000032:analysis*; D013743:Tetanus Antitoxin
D013301:Streptolysins; D013743:Tetanus Antitoxin; D009243:NAD; D012967:Sodium Dodecyl Sulfate; D009699:N-Glycosyl Hydrolases