Purification and Characterization of an Extracellular Proteinase from Brevibacterium linens ATCC 9174.

Abstract:

:An extracellular serine proteinase from Brevibacterium linens ATCC 9174 was purified to homogeneity. pH and temperature optima were 8.5 and 50(deg)C, respectively. The results for the molecular mass of the proteinase were 56 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 126 kDa by gel filtration, indicating that the native enzyme exists as a dimer. Mg(sup2+) and Ca(sup2+) activated the proteinase, as did NaCl; however, Hg(sup2+), Fe(sup2+), and Zn(sup2+) caused strong inhibition. The sequence of the first 20 N-terminal amino acids was NH(inf2)-Ala-Lys-Asn-Asp-Ala-Val-Gly-Gly-Met-Gly-Tyr-Leu-Ser-Met-Ile-Pro-Se r-Gln-Pro-Gly.

journal_name

Appl Environ Microbiol

authors

Rattray FP,Bockelmann W,Fox PF

doi

10.1128/AEM.61.9.3454-3456.1995

keywords:

subject

Has Abstract

pub_date

1995-09-01 00:00:00

pages

3454-6

issue

9

eissn

0099-2240

issn

1098-5336

journal_volume

61

pub_type

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