Comparative study of the neutral proteinases from fungi and actinomycetes using polyacrylamide gel electrophoresis.
Neutral proteinases from mycelial extracts of fungi and actinomycetes may be readily detected by polyacrylamide gel electrophoresis in which azocasein is incorporated into the gels. Most of the proteinases detectable at pH 6.5 were sensitive to both phenylmethanesulphonyl fluoride and to mercuric chloride. In all the species examined, except for one, the proteinase activities in the mycelial extracts increased during storage at 19 degrees C.
D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000032:analysis* / Q000378:metabolism; D004789:Enzyme Activation; D005658:Fungi / Q000201:enzymology*; D008627:Mercuric Chloride / Q000494:pharmacology; D008666:Metalloendopeptidases; D010664:Phenylmethylsulfonyl Fluoride / Q000494:pharmacology; D011480:Protease Inhibitors; D013045:Species Specificity; D013302:Streptomyces / Q000201:enzymology*
D011480:Protease Inhibitors; D008627:Mercuric Chloride; D010664:Phenylmethylsulfonyl Fluoride; D010450:Endopeptidases; D008666:Metalloendopeptidases