Proteinase activity in rumen ciliate protozoa.
Azocasein-degrading proteinase activity was detected in all rumen ciliate protozoa that were examined from four entodiniomorphid and two holotrich genera. All of the activities were optimal in the range pH 4.0-5.0 and were inhibited by cysteine proteinase inhibitors, notably leupeptin. The inhibition profiles and extent of inhibition observed with the different groups of inhibitors were organism-specific. Gelatin-SDS-polyacrylamide gel electrophoresis of protozoal lysates revealed multiple forms of the proteinases in the species examined. The number of enzymes detected, their molecular masses, the level of activity and inhibitor susceptibility was genus-dependent. The proteinase profiles of the two holotrich species differed and inter-species differences were also apparent among species of the genus Entodinium. The characteristics and molecular size distribution of rumen bacterial proteinases were different to the protozoal proteinases. Low levels of proteinase activity, of apparently bacterial origin, were detected by gelatin-SDS-PAGE analysis of cell-free rumen liquor.
Lockwood
B C
BC
Department of Zoology, University of Glasgow, UK.
Coombs
G H
GH
Williams
A G
AG
D000818:Animals; D001419:Bacteria / Q000201:enzymology; D002364:Caseins / Q000378:metabolism; D016798:Ciliophora / Q000187:drug effects / Q000201:enzymology*; D015853:Cysteine Proteinase Inhibitors; D010450:Endopeptidases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007976:Leupeptins / Q000494:pharmacology; D012417:Rumen / Q000382:microbiology*; D012756:Sheep; D013045:Species Specificity
D002364:Caseins; D015853:Cysteine Proteinase Inhibitors; D007976:Leupeptins; C026018:azocasein; D010450:Endopeptidases