Premium
An inventory of peptide hydrolases and arylamidases in Flavobacterium II b
Author(s) -
Milliere J.B.,
VeilletPoncet L.
Publication year - 1985
Publication title -
journal of applied bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.889
H-Index - 156
eISSN - 1365-2672
pISSN - 0021-8847
DOI - 10.1111/j.1365-2672.1985.tb03346.x
Subject(s) - dipeptidase , aminopeptidase , flavobacterium , trypsin , biochemistry , chymotrypsin , exopeptidase , chemistry , peptide , carboxypeptidase , hydrolysis , leucine , amidase , enzyme , electrophoresis , amino acid , biology , bacteria , pseudomonas , genetics
The determination of the number and the specificity of peptide hydrolases and arylamidases present in a cell‐free sonicate from Flavobacterium II b, a species phenotypically similar to Flavobacterium balustinum , involved polyacrylamide gel electrophoresis and coloration of end products or staining procedures using diazotation reactions. Only substrates with L‐configuration amino acids and dipeptides with an unsubstituted R N ‐group were cleaved. One protein band, that was able to hydrolyse skimmed milk agar, was observed but carboxypeptidase and endopep‐tidase (chymotrypsin and trypsin activities) were absent. Zymograms exhibited ary‐lamidase, dipeptidase and tripeptidase activities. Results underline the distinction between the L‐leucine aminopeptidase and the L‐leucylarylamidase.