膵臓性エラスターゼの酵素化学的研究(第2報)ブタ膵臓性エラスターゼIのフィブロネクチン水解作用について

概要

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Proteolytic actions of hog pancreatic elastase I on plasma fibronectin, in vitro, were analyzed by SDS-polyacrylamide gel electrophoresis. The enzyme was incubated with fibronectin, at the ratio of 1 : 100 (w : w) (=molar ratio, 1 : 6), at 37℃, pH 7.4 for various periods. Intact fibronectin molecule (molecular weight : ca. 450 kilodaltons (kd)) was completely digested within 5 min incubation, and five major fragments having the molecular weights of 180,160,130,60,and 25 kd were newly generated. After 4 h incubation, fragments of 180,160,130,60 kd gradually disappeared, and fragments of 75,50 and 35 kd were newly detected. Two fragments out of these peptide fragments, i.e., 60 and 50 kd fragments retained gelatin-binding activity. It is, therefore, assumed that the 50 kd fragment was derived from the early 60 kd fragment. These elastase activities were suppressed by 150 mM sodium chloride, i.e., even after 2 h incubation, 60 and 130 kd fragments remained in quantity and 75,50,and 35 kd fragments were not generated. Elastatinal strongly inhibited the proteolytic actions of elastase on fibronectin.
公益社団法人日本薬学会の論文
1984-07-25