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PMID: 743235 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

The exocellular DD-carboxypeptidase-endopeptidase from Streptomyces albus G. Purification and chemical properties.

The Biochemical journal ·Vol. 175 ·No. 3 ·1978-12-01 ·Pages 793-800

Duez C, Frère JM, Geurts F, Ghuysen JM, Dierickx L, Delcambe L

Abstract

The exocellular DD-carboxypeptidase-endopeptidase of Streptomyces albus G was purified to protein homogeneity and compared with the exocellular DD-carboxypeptidases-transpeptidases of Streptomyces R61 and Actinomadura R39. The S. albus G enzyme, as it is isolated, occurs in two forms. Enzyme I (30% of the total amount) and enzyme II (70% of the total amount) are identical in all respects, except that, by polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate, enzyme I has an apparent mol. wt. (9000) that is half of that found by molecular-sieve filtration under non-denaturing conditions. Irrespective of the technique used, enzyme II has an apparent mol. wt. of about 18500.

MeSH Terms
Alanine Amino Acids/analysis Chromatography, Gel Dipeptidases Dipeptides Electrophoresis, Polyacrylamide Gel Endopeptidases/isolation & purification Extracellular Space/enzymology Molecular Weight Spectrum Analysis Streptomyces/enzymology
Chemicals
Amino Acids Dipeptides Endopeptidases Dipeptidases DD-carboxypeptidase-endopeptidase Alanine
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Duez C
Frère J M
Geurts F
Ghuysen J M
Dierickx L
Delcambe L
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19 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj1750793
Published
1978-12-01
Pages
793-800
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1186139
Subset
IM
External Links
PubMed source DOI: 10.1042/bj1750793 PMC Full Text View journal details
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