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PMID: 1218078 Published · ppublish English Comparative Study Journal Article

The amino acid sequence of Staphylococcus aureus penicillinase.

The Biochemical journal ·Vol. 151 ·No. 2 ·1975-11-00 ·Pages 197-218

Ambler RP

Abstract

The amino acid sequence of the penicillinase (penicillin amido-beta-lactamhydrolase, EC 3.5.2.6) from Staphylococcus aureus strain PC1 was determined. The protein consists of a single polypeptide chain of 257 residues, and the sequence was determined by characterization of tryptic, chymotryptic, peptic and CNBr peptides, with some additional evidence from thermolysin and S. aureus proteinase peptides. A mistake in the preliminary report of the sequence is corrected; residues 113-116 are now thought to be -Lys-Lys-Val-Lys- rather than -Lys-Val-Lys-Lys-. Detailed evidence for the amino acid sequence has been deposited as Supplementary Publication SUP 50056 (91 pages) at the British Library (Lending Division), Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1975) 145, 5.

MeSH Terms
Amides/analysis Amino Acid Sequence Chromatography, Gel Chromatography, Ion Exchange Culture Media Cyanogen Bromide Electrophoresis, Starch Gel Penicillinase/analysis,isolation & purification Peptide Hydrolases Staphylococcus aureus/enzymology Tetranitromethane
Chemicals
Amides Culture Media Peptide Hydrolases Penicillinase Tetranitromethane Cyanogen Bromide
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Ambler R P
References (20)
20 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1975-11-00
Pages
197-218
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1172349
Subset
IM
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