A potent inhibitor of pancreatic serine proteases from chick skeletal muscle
1990
Kim, O.M. | Chung, S.S. | Park, H.G. | Chung, C.H. | Ha, D.B. (Seoul National Univ., Seoul (Korea Republic). Coll. of Natural Sciences) | Choe, J.H. (Korea Advanced Inst. of Science and Engineering , Taejon (Korea Republic))
A potent inhibitor of trypsin and other various serine proteases including chymotrypsin, elastase, kallikrein, plasmin and subtilisin, has been purified to homogeneity from chick skeletal muscle by conventional chromatographic procedures. The inhibitor has an apparent molecular weight of 66,000 dalton as determined by gel filtration. When the purified inhibitor was electrophoresed in the presence of sodium dodecyl sulfate, there appeared two protein bands having molecular weights of 66,000 and 64,000 dalton. The 64,000 dalton protein seems to be the product of 66,000 dalton protein by a limited proteolysis during the purification procedure or in vivo. Thus, it seems to consist of a single polypeptide. The inhibitor appeared to be glycoprotein and have an isoelectric point of 7.4. It contains relatively large amount (8.33 mole %) of cysteine residues
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