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Purification and characterization of an extracellular proteinase from Brevibacterium linens ATCC 9174
An extracellular serine proteinase from Brevibacterium linens ATCC 9174 was purified to homogeneity. pH and temperature optima were 8.5 and 50 degrees C, respectively. The results for the molecular mass of the proteinase were 56 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 12...
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Published in: | Applied and Environmental Microbiology 1995-09, Vol.61 (9), p.3454-3456 |
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creator | Rattray, F.P. (University College, Cork, Ireland.) Bockelmann, W Fox, P.F |
description | An extracellular serine proteinase from Brevibacterium linens ATCC 9174 was purified to homogeneity. pH and temperature optima were 8.5 and 50 degrees 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. Mg2+ and Ca2+ activated the proteinase, as did NaCl; however, Hg2+, Fe2+, and Zn2+ caused strong inhibition. The sequence of the first 20 N-terminal amino acids H2-Ala-Lys-Asn-Asp-Ala-Val Gly-Gly-Met-Gly-Tyr-Leu-Ser-Met-Ile-Pro-Ser-Gln-pro-Gly |
doi_str_mv | 10.1128/aem.61.9.3454-3456.1995 |
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(University College, Cork, Ireland.)</creatorcontrib><creatorcontrib>Bockelmann, W</creatorcontrib><creatorcontrib>Fox, P.F</creatorcontrib><title>Purification and characterization of an extracellular proteinase from Brevibacterium linens ATCC 9174</title><title>Applied and Environmental Microbiology</title><addtitle>Appl Environ Microbiol</addtitle><description>An extracellular serine proteinase from Brevibacterium linens ATCC 9174 was purified to homogeneity. pH and temperature optima were 8.5 and 50 degrees 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. Mg2+ and Ca2+ activated the proteinase, as did NaCl; however, Hg2+, Fe2+, and Zn2+ caused strong inhibition. 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(University College, Cork, Ireland.) ; Bockelmann, W ; Fox, P.F</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c600t-8d7d2db2b7becdd575a673163befb236e48e62750156efaad160af8431bb8f853</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>ACTIVIDAD ENZIMATICA</topic><topic>ACTIVITE ENZYMATIQUE</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Biology of microorganisms of confirmed or potential industrial interest</topic><topic>Biotechnology</topic><topic>BREVIBACTERIUM LINENS</topic><topic>Cellular biology</topic><topic>COMPOSICION QUIMICA</topic><topic>COMPOSITION CHIMIQUE</topic><topic>Enzymes</topic><topic>Fundamental and applied biological sciences. 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subjects | ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE Bacteriology Biological and medical sciences Biology of microorganisms of confirmed or potential industrial interest Biotechnology BREVIBACTERIUM LINENS Cellular biology COMPOSICION QUIMICA COMPOSITION CHIMIQUE Enzymes Fundamental and applied biological sciences. Psychology Mission oriented research Physiology and metabolism PROTEASAS PROTEASE Proteins PROTEOLISIS PROTEOLYSE PURIFICACION PURIFICATION |
title | Purification and characterization of an extracellular proteinase from Brevibacterium linens ATCC 9174 |
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