<原著>モルモット血漿中のシステインプロテイナーゼインヒビター : その精製, 性質および急性相反応

概要

論文の詳細を見る
Two kinds of low molecular weight kininogen (LK1 and LK2) and one kind of high molecular weight kininogen (HK) were isolated to an apparently homogeneous state from pooled plasma of guinea pigs. The molecular weights of LK1,LK2 and HK were calculated to be 65,000,60,000,80,000,respectively. When polyclonal antisera raised against the individual proteins were used, immunological cross-reactions were observed between LK1 and HK, but not between LK1 and LK2 or between LK2 and HK. LK1 and LK2 were glycoproteins having 23.7 and 23.5% carbohydrate, respectively. The protein relatedness between LK1 and LK2 was calculated as 23.3 SΔQ, suggesting that LK1 and LK2 were similar proteins. The kininogens inhibited cysteine proteinases such as papain and ficin but they did not inhibit trypsin. When incubated with kallikrein or trypsin for 30 min at 37℃, each kininogen released kinin. When the acute phase reaction was induced by subcutaneous injection of turpentine, the LK1 concentration doubled while those of LK2 and HK remained relatively unchanged. These results indicate that the guinea pig differs from other species in the nature of kininogens and in the acute phase response.
近畿大学の論文
1990-03-25