Purification and Characterization of an Extracellular Proteinase from Brevibacterium-Linens ATCC-9174

TY - GEN

T1 - Purification and Characterization of an Extracellular Proteinase from Brevibacterium-Linens ATCC-9174

AU - Rattray, F P

AU - Bockelmann, W

AU - Fox, P F

PY - 1995

Y1 - 1995

N2 - 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 was NH2-Ala-Lys- Asn-Asp-Ala-Val-Gly-Gly-Met-Gly-Tyr-Leu-Ser-Met-IIe-Pro-Ser-Gln- Pro-Gly

AB - 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 was NH2-Ala-Lys- Asn-Asp-Ala-Val-Gly-Gly-Met-Gly-Tyr-Leu-Ser-Met-IIe-Pro-Ser-Gln- Pro-Gly

KW - ACID

KW - ACIDS

KW - AMINO-ACID

KW - AMINO-ACIDS

KW - Amino Acid

KW - Amino Acids

KW - Brevibacterium

KW - CHEESE

KW - Characterization

KW - ENZYME

KW - Electrophoresis

KW - Extracellular Proteinase

KW - GEL-ELECTROPHORESIS

KW - Gel

KW - INHIBITION

KW - KDA

KW - Molecular

KW - PROTEINASE

KW - PURIFICATION

KW - SEQUENCE

KW - SERINE PROTEINASE

KW - Serine

KW - Temperature

KW - Zn2+

M3 - Other contribution

VL - Vol 61

ER -