Purification of Tissue Activator of Plasminogen and Its Effect on Enhancement of Permeability in Rabbit Skin

概要

論文の詳細を見る
1) An attempt was made to find out a method to purify plasminogen activator from rabbit kidney. The activator could be extracted from the lysosome-rich fraction with universal buffer, pH 10.5, and the proteolytic activity could be isolated from the activator by alkaline extraction. The alkaline extraction, followed by chromatography on DEAE-cellulose with stepwise increase in concentration of KCI solution, gave 51 fold purification of the activator. Three major protein peaks (peak I, peak II and peak III) were eluted with three stepwise increase in concentration of KCI. Almost 60% of the activator activity was eluted with 0.1 M-KCI sglution in peak II, which. showed esterase activity against L-histidine methyl ester, and peak I was esterolytic against L-lysine ethyl ester and eluted with 0.05M-KCI solution.<BR>2) The purified activator (peak II) was intracutaneously active as aninducer of extravasation of trypan blue in a localized skin area of the rabbit, and, on the other hand, peak I was not active as an inducer.<BR>3) Aminomethylcyclohexanecarboxylic acid strongly inhibited the activator activity against caseinolysis and fibrin clot lysis of plasminogen. L-Histidine hexyl and benzyl ester also inhibited the activator activity against caseinolysis, but did not inhibit fibrin clot lysis. These compounds showed the anti-inflammatory activity to the enhancement of permeability in the rabbit skin.