title: Partial Purification of Mucor pusillus Intracellular Proteases.
abstract: The intracellular protease extracted from the freeze-dried mycelia obtained after the growth of Mucor pusillus at 30 degrees C in corn steep liquor medium was chromatographed on DEAE-A50. Some characteristics of the protease fractions obtained after ion-exchange chromatography were determined and compared with those of the extracellular proteases reported previously. The mycelia were found to contain two acid proteases and an alkaline protease. The ratio of milk clotting to protease activity of one acid protease was greater than that of the other. The electrophoretic pattern of the alkaline protease fraction suggested that it was not a single species, but a mixture of proteolytic enzymes.
authors.affiliation: Department of Biochemistry, Strathclyde University, Glasgow, Scotland.
authors.forename: M R
authors.initials: MR
authors.lastname: Khan
authors.forename: J A
authors.initials: JA
authors.lastname: Blain
authors.forename: J D
authors.initials: JD
authors.lastname: Patterson