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Biomedical subjects

J A Blain

Publications and source records attributed to J A Blain.

5 recordsLinked to original sources
PubMed1983

Partial Purification of Mucor pusillus Intracellular Proteases.

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.

Journal Article↗
PubMed1979

Extracellular Proteases of Mucor pusillus.

Mucor pusillus was grown in different media for a period of 92 h, and the media were investigated for both milk-clotting and protease activities. It was observed that the ratio of extracellular milk-clotting activity to protease activity was the highest for 3% corn steep liquor containing 1% glucose as the source of carbon. Variation of both milk-clotting and protease activities was studied during the growth of the organism in the medium stated above. Separation of protease was carried out by ion-exchange chromatography at pH 8.0. Fractions collected were assayed for both activities simultaneously. The findings suggested that, instead of only one major acid protease, as reported by previous workers, two major acid proteases were produced. One of them had significant rennin-like activity, and the other lacked it. The former could be assumed to be the enzyme reported and studied by previous workers. The existence of two proteases was further confirmed by the appearance of two protease activity bands on polyacrylamide gels after electrophoresis. An attempt was made to separate the rennin-like enzyme from nonspecific protease activity by ammonium sulfate fractionation followed by ion-exchange chromatography at pH 6.0. The results indicated that the nonspecific protease activity due to the enzyme that lacked rennin action was substantially removed by the ammonium sulfate fractionation.

Journal Article↗
PubMed1976

Study of bound phospholipase activities of fungal mycelia using an organic solvent system.

It has been possible to demonstrate and characterize high phospholipase activities in mycelia of Rhizopus arrhizus and Mucor javanicus by use of a system in which substrates were dissolved in diisopropyl ether. Such activities were associated with bound enzymes and would have been difficult to detect using aqueous assay systems. In both cases, phosphatidylcholine hydrolysis was by phospholipase A1 (EC 3.1.1.32) activity followed by the action of lysophospholipase (EC 3.1.1.5). Phospholipase D (EC 3.1.4.4) activity was also detected. The methods used appear to be of general applicability for the detection and study of insoluble phospholipases.

Animals↗