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KMID : 0364219900330010119
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Korean Journal of Zoology
1990 Volume.33 No. 1 p.119 ~ p.125
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A Potent Inhibitor of Pancreatic Serine Proteases from Chick Skeletal Muscle
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Kim Ok-Mae
Chung Sung-Soo
Park Hye-Gyeong
Choe Joon-Ho
Chung Chin-Ha
Ha Doo-Bong
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Abstract
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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 convendonal 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 rwo 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 lin'ited proteolysis during the purification procedure or in viuo. 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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KEYWORD
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Trypsin , Serine , proteases , Ingibitor
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