Purification and partial characterization of the nephritis strain-associated protein from Streptococcus pyogenes, group A.
We report the isolation and purification of the nephritis strain-associated protein (NSAP) first described by Villareal et al. (8). Amino acid analysis, and determination of the first 21 amino-terminal amino acids indicated that this 46 kD protein is a streptokinase. Biochemical analysis confirmed that NSAP could act as a plasminogen activator; immunological investigations indicated that NSAP is antigenically different from streptokinase from group C streptococcus, and possibly represents a unique streptokinase. It is this uniqueness that may contribute to the role of NSAP in the pathogenesis of acute poststreptococcal glomerulonephritis.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000911:Antibodies, Monoclonal; D001426:Bacterial Proteins / Q000276:immunology / Q000302:isolation & purification*; D002845:Chromatography; D005921:Glomerulonephritis / Q000382:microbiology*; D007163:Immunosorbent Techniques; D008970:Molecular Weight; D010960:Plasminogen Activators / Q000032:analysis; D013297:Streptococcus pyogenes / Q000032:analysis* / Q000472:pathogenicity; D013300:Streptokinase / Q000032:analysis / Q000276:immunology
D000596:Amino Acids; D000911:Antibodies, Monoclonal; D001426:Bacterial Proteins; C042387:nephritis-strain associated protein, group A Streptococcus; D013300:Streptokinase; D010960:Plasminogen Activators