Purification and characterization of rhizopuspepsin isozymes from a liquid culture of Rhizopus chinensis.
1. Rhizopuspepsin has been purified from liquid cultures of Rhizopus chinensis. 2. Purification by ammonium sulfate precipitation, affinity chromatography on pepstatin Sepharose and low/high resolution isoelectric focusing produced five isoelectric forms. 3. The two major isozymes pI 5.1 and 5.8 did not differ significantly in amino acid composition, molecular weight and enzyme activity. 4. Three minor isozymes were partially purified as pI 7.35, 7.41 and 7.9.
D016282:Aspartic Acid Endopeptidases; D055598:Chemical Phenomena; D002621:Chemistry; D002846:Chromatography, Affinity; D003470:Culture Media; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000302:isolation & purification*; D007525:Isoelectric Focusing; D007527:Isoenzymes / Q000302:isolation & purification*; D012233:Rhizopus / Q000201:enzymology*
D003470:Culture Media; D007527:Isoenzymes; D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases; C035794:rhizopuspepsin