Proteinase inhibitors in hamster plasma: Purification, properties and acute phase response

publisher学位の種類：医学 学位授与年月日：1992/6/15 指導： 篠原, 兵庫 教授(Director: Prof. Sinohara, Hyogo) 報告番号：乙第172号 学内授与番号：医乙123 NDL書誌ID：000000266542[ABSTRACT] 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-a-trypsin inhibitor had a molecular mass of 55 kDa and 120 kDa, respectively, and both inhibited only trypsin. The pre-a-trypsin inhibitor consisted of light —1—(25 kDa) and heavy (90 kDa) polypeptide chains, which were dissociated by chondroitinase ABC treatment but not by heating at 100℃ 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