Aminopeptidase I activities in several microorganisms.
Can J Biochem
; 56(1): 66-71, 1978 Jan.
Article
em En
| MEDLINE
| ID: mdl-110425
ABSTRACT
Aminopeptidase I activity which was found to be localized in the same subcellular fraction and to be similarly heat stable was partially purified by a common procedure from Escherichia coli B, Escherichia coli K12, Enterobacter aerogenes, Salmonella typhimurium, Serratia marcescens Pseudomonas aeruginosa, and Proteus vulgaris. The enzyme preparations were shown to contain a single animopeptidase active toward both leucylleucine and methionylalanylserine by mixed-substrate initial-velocity kinetic analysis. The Km value for leucylleucine was virtually identical for the aminopeptidases of all of the organisms, as was the Km value for methionylalanylserine.
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Coleções:
01-internacional
Contexto em Saúde:
3_ND
Base de dados:
MEDLINE
Assunto principal:
Bactérias
/
Aminopeptidases
Idioma:
En
Revista:
Can J Biochem
Ano de publicação:
1978
Tipo de documento:
Article