Protein characterizations and immunological properties of the low-molecular-mass protein A isolated from Staphylococcus aureus KS 1034.
The extracellular low-molecular-mass protein A isolated from Staphylococcus aureus KS 1034 was analyzed for its amino acid contents and terminal amino acid sequences. The C-terminal and the N-terminal amino acid sequences of the low-molecular-mass protein A were -Asn-Ala-Phe and Ala-Gln-His-Asp-Glu-Ala-Gln-, respectively. For immunochemical properties, the low-molecular-mass protein A was similar to protein A isolated from S. aureus Cowan I. Extracellular protease activity of KS 1034 strain was considerably lower than S. aureus C-30 isolated from chicken that produced the extracellular low-molecular-mass protein A.
Kusunoki
H
H
Department of Chemistry, Nippon Veterinary and Animal Science University, Tokyo, Japan.
Hara
N
N
Saito
K
K
Hasuda
K
K
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D010450:Endopeptidases / Q000378:metabolism; D015151:Immunoblotting; D005779:Immunodiffusion; D007150:Immunohistochemistry; D008969:Molecular Sequence Data; D013205:Staphylococcal Protein A / Q000737:chemistry* / Q000276:immunology; D013211:Staphylococcus aureus / Q000737:chemistry* / Q000276:immunology
D000596:Amino Acids; D013205:Staphylococcal Protein A; D010450:Endopeptidases