[Separation and characteristics of the proteolytic enzymes of Bacillus subtilis].
The composition of two protosubtilins -- proteolytic enzymes of the enzymes isolated from submerged cultures of two Bacillus subtilis strains was investigated. Each of the preparations contained two proteinases that differed in their pH optimum. Conditions of chromatographic separation of two proteinases on CM-52 cellulose were tested. With the use of specific inhibitors and specific substrates it has been shown that one of the proteinases belongs to metal enzymes and is inhibited by ethylene diamine tetracetate (EDTA). Another proteinase, which is probably serine proteinase, is inhibited by diazopropine fluorophosphate (DFP). The isoelectric point of neutral proteinase is 8.15-8.20.
D001412:Bacillus subtilis / Q000201:enzymology*; D002852:Chromatography, Ion Exchange; D004492:Edetic Acid / Q000494:pharmacology; D004794:Enzyme Repression / Q000187:drug effects; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D007531:Isoflurophate / Q000494:pharmacology; D010447:Peptide Hydrolases / Q000032:analysis; D013381:Subtilisins / Q000037:antagonists & inhibitors / Q000302:isolation & purification*
D007531:Isoflurophate; D004492:Edetic Acid; D010447:Peptide Hydrolases; D013381:Subtilisins
Razdelenie i kharakteristika proteoliticheskikh fermentov Bacillus subtilis