Isolation and study of an inhibitor of the intrinsic proteolytic enzyme of cotton seeds
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A scheme has been developed for the isolation of an inhibitor of cottonseed protease A using affinity chromatography on protease-A—Sepharose 4B followed by gel filtration on Sephadex G-150. The molecular mass of the inhibitor is 20 kDa. The protein molecule consists of two subunits with different molecular masses.
KeywordsAmino Acid Composition Cotton Seed Isoleucine Leucine Pyridine Acetate Pyridine Acetate Buffer
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