<原著>ハムスター血漿中のプロテイナーゼインヒビター : 精製と性質および急性相反応
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概要
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In this study three proteins with trypsin inhibitory activity were purified to apparent homogeneity from hamster plasma and the changes in their plasma level after acute inflammation were examined. α-1-Antiproteinase had a molecular mass of 68 kDa, and inhibited elastase, trypsin and chymotrypsin but not plasmin, porcine pancreas kallikrein or guinea pig plasma kallikrein. Countertrypin and pre-α-trypsin inhibitor had a molecular mass of 55 kDa and 120 kDa, respectively, and both inhibited only trypsin. The pre-α-trypsin inhibitor consisted of light (25 kDa) and heavy (90 kDa) polypeptide chains, which were dissociated by chondroitinase ABC treatment but not by heating at 10O℃ in the presence of sodium dodecyl sulfate and dithiothreitol. Thirteen amino acids of the N-terminal eicosapeptide sequence of both light and heavy chains were identical with the corresponding regions of human serum pre-α-trypsin inhibitor. After induction of inflammation by intraperitoneal injection of Salmonella typhimurium lipopolysaccharide, the plasma level of pre-α-trypsin inhibitor increased and that of murinoglobulin decreased, but other inhibitors showed no significant change.
- 近畿大学の論文
- 1992-06-25