Specificity of an extracellular proteinase from Brevibacterium linens ATCC 9174 on bovine alphas1-casein

The specificity of the extracellular proteinase from Brevibacterium linens ATCC 9174 on bovine alpha s1-casein was studied. Hydrolysis was monitored over time by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (PAGE) and urea-PAGE. The major pH 4.6-soluble peptides were isolated by high-pe...

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Bibliographic Details
Published inApplied and environmental microbiology Vol. 62; no. 2; p. 501
Main Authors Rattray, F.P. (University College, Cork, Ireland.), Fox, P.F, Healy, A
Format Journal Article
LanguageEnglish
Published Washington American Society for Microbiology 01.02.1996
Subjects
ACTIVIDAD ENZIMATICA
ACTIVITE ENZYMATIQUE
Amino acids
Bacteria
BOVIN
BREVIBACTERIUM LINENS
Cellular biology
COMPOSICION QUIMICA
COMPOSITION CHIMIQUE
GANADO BOVINO
HIDROLISIS
HYDROLYSE
PROTEASAS
PROTEASE
Proteins
PROTEOLISIS
PROTEOLYSE
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Summary:The specificity of the extracellular proteinase from Brevibacterium linens ATCC 9174 on bovine alpha s1-casein was studied. Hydrolysis was monitored over time by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (PAGE) and urea-PAGE. The major pH 4.6-soluble peptides were isolated by high-performance liquid chromatography and identified by N-terminal amino acid sequencing and mass spectrometry. The time course of peptide formation indicated that His-8-Gln-9, Ser-161-Gly-162, and either Gln-172-Tyr-173 or Phe-23-Phe-24 were the first, second, and third bonds cleaved, respectively. Other cleavage sites included Asn-19-Leu-20, Phe-32-Gly-33, Tyr-104-Lys-105, Leu-142-Ala-143, Phe-150-Arg-151, Gln-152-Phe-153, Leu-169-Gly-170, and Thr-171-Gln-172. The proteinase had a broad specificity for the amino acid residues at the P1 and P'1 positions but showed a preference for hydrophobic residues at the P2, P3, P4, P'2, P'3, and P'4 positions
Bibliography:Q02
9605086
ISSN:0099-2240
1098-5336