| http://purl.uniprot.org/citations/7632397 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7632397 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7632397 | http://www.w3.org/2000/01/rdf-schema#comment | "Alkaline protease (EC 3.4.21.14) activity, suitable for use in detergents, was detected in the alkaline culture medium of Bacillus sp. KSM-K16, which was originally isolated from soil. The enzyme, designated M protease, was purified to homogeneity from the culture broth by column chromatographies. The N-terminal amino acid sequence was Ala-Gln-Ser-Val-Pro-Trp-Gly-Ile-Ser-Arg-Val-Gln-Ala-Pro-Ala-Ala-His-Asn-Arg-Gly-Leu-Thr-Gly. The molecular mass of the protease was 28 kDa, and its isoelectric point was close to pH 10.6. Maximum activity toward casein was observed at 55 degrees C and at pH 12.3 in 50 mM phosphate/NaOH buffer. The activity was inhibited by phenylmethylsulfonyl fluoride and chymostatin. The enzyme was very stable in long-term incubation with liquid detergents at 40 degrees C. The enzyme cleaved the oxidized insulin B chain initially at Leu15-Tyr16 and efficiently at ten more sites. Among various oligopeptidyl p-nitro-anilides (pNA) tested, N-succinyl-Ala-Ala-Pro-Phe-pNA was efficiently hydrolyzed by M protease. M protease was precipitated in (NH4)2SO4-saturated acetate buffer (pH 5.0) as plank-like crystals."xsd:string |
| http://purl.uniprot.org/citations/7632397 | http://purl.org/dc/terms/identifier | "doi:10.1007/bf00218452"xsd:string |
| http://purl.uniprot.org/citations/7632397 | http://purl.org/dc/terms/identifier | "doi:10.1007/bf00218452"xsd:string |
| http://purl.uniprot.org/citations/7632397 | http://purl.org/dc/terms/identifier | "doi:10.1007/s002530050437"xsd:string |
| http://purl.uniprot.org/citations/7632397 | http://purl.uniprot.org/core/author | "Kobayashi T."xsd:string |
| http://purl.uniprot.org/citations/7632397 | http://purl.uniprot.org/core/author | "Kobayashi T."xsd:string |
| http://purl.uniprot.org/citations/7632397 | http://purl.uniprot.org/core/author | "Adachi S."xsd:string |
| http://purl.uniprot.org/citations/7632397 | http://purl.uniprot.org/core/author | "Adachi S."xsd:string |
| http://purl.uniprot.org/citations/7632397 | http://purl.uniprot.org/core/author | "Ito S."xsd:string |
| http://purl.uniprot.org/citations/7632397 | http://purl.uniprot.org/core/author | "Ito S."xsd:string |
| http://purl.uniprot.org/citations/7632397 | http://purl.uniprot.org/core/author | "Kawai S."xsd:string |
| http://purl.uniprot.org/citations/7632397 | http://purl.uniprot.org/core/author | "Kawai S."xsd:string |
| http://purl.uniprot.org/citations/7632397 | http://purl.uniprot.org/core/author | "Koike K."xsd:string |
| http://purl.uniprot.org/citations/7632397 | http://purl.uniprot.org/core/author | "Koike K."xsd:string |
| http://purl.uniprot.org/citations/7632397 | http://purl.uniprot.org/core/author | "Hitomi J."xsd:string |
| http://purl.uniprot.org/citations/7632397 | http://purl.uniprot.org/core/author | "Hitomi J."xsd:string |
| http://purl.uniprot.org/citations/7632397 | http://purl.uniprot.org/core/author | "Hakamada Y."xsd:string |
| http://purl.uniprot.org/citations/7632397 | http://purl.uniprot.org/core/author | "Hakamada Y."xsd:string |
| http://purl.uniprot.org/citations/7632397 | http://purl.uniprot.org/core/author | "Yoshimatsu T."xsd:string |
| http://purl.uniprot.org/citations/7632397 | http://purl.uniprot.org/core/author | "Yoshimatsu T."xsd:string |
| http://purl.uniprot.org/citations/7632397 | http://purl.uniprot.org/core/date | "1995"xsd:gYear |
| http://purl.uniprot.org/citations/7632397 | http://purl.uniprot.org/core/date | "1995"xsd:gYear |
| http://purl.uniprot.org/citations/7632397 | http://purl.uniprot.org/core/name | "Appl. Microbiol. Biotechnol."xsd:string |