Isolation and study of an inhibitor of the intrinsic proteolytic enzyme of cotton seeds
- 20 Downloads
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
Unable to display preview. Download preview PDF.
- 1.V. V. Mosolov, Vopr. Med. Khim.,52 (1987).Google Scholar
- 2.M. A. Belozerskii, Ya. E. Dunaevskii, and N. E. Voskoboinikova, Dokl. Akad. Nauk SSSR,264, 991 (1982)Google Scholar
- 3.E. P. Shapenko, Neutral Proteases of Wheat Grain and Their Protein Inhibitors, Author's abstract of dissertation for Candidate of Biological Sciences [in Russian], MTIP [Moscow Technological Institute of the Food Industry], Moscow (1980).Google Scholar
- 4.I. A. Tipisova, Proteolytic Enzymes of Soybeans, Author's abstract of dissertation for Candidate of Biological Sciences [in Russian], MTIPP, Moscow (1981).Google Scholar
- 5.L. G. Mezhlum'yan, M. A. Kuchenkova, and P. Kh. Yuldashev, Khim. Prir. Soedin., 738 (1986).Google Scholar
- 6.L. G. Mezhlum'yan and P. Kh. Yuldashev, Khim. Prir. Soedin., 109 (1991).Google Scholar
- 7.A. M. Yumaleev and R. I. Ibragimov, Dokl. VASKhNIL [All-Union Academy of Agricultural Sciences], 9 (1986).Google Scholar
- 8.B. G. Davis, Ann. N.Y. Acad Sci., 404 (1964).Google Scholar