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- W4240218178 abstract "Aminopeptidase C was purified from fresh chicken skeletal muscle by ammonium sulfate fractionation, and by successive chromatography on DEAE-cellulose, Ultrogel AcA 34, DEAE-cellulose again, and an alanine AH-Sepharose 4B affinity column twice. The purified enzyme migrated as a single band by SDS-PAGE. Aminopeptidase C was purified about 300-fold over the crude extract with a yield of 0.6%. The molecular weight of this enzyme was found to be 185, 000 by gel filtration in a Sepharose 6B column and 92, 000 by SDS-PAGE. The optimum pH for the hydrolysis of L-leucine β-naphthylamide was 6.0-7.0, the enzyme being stable in the range of pH 6.5-8.0. The activity of this enzyme was strongly inhibited by EDTA and puromycin, and was high against the β-naphthylamide derivatives of Lys, Leu, Ala and Met. The enzyme was more active towards tri- and tetrapeptides than towards dipeptides." @default.
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- W4240218178 date "1991-01-01" @default.
- W4240218178 modified "2023-10-01" @default.
- W4240218178 title "Purification and Properties of Aminopeptidase C from Chicken Skeletal Muscle." @default.
- W4240218178 doi "https://doi.org/10.1271/bbb1961.55.1771" @default.
- W4240218178 hasPublicationYear "1991" @default.
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