膵臓性エラスターゼの酵素化学的研究(第3報)血液中に移行する膵臓由来の前駆体様エラスターゼについて

概要

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It has become apparent that trypsin activatable inactive elastase was present in the hog blood. 1) After anti-hog pancreatic elastase I antibody-Sepharose 4B immunoaffinity chromatography, about 9 μg of inactive elastase was detected with enzymic activity in 11 of citrated hog plasma. 2) The inactive latent enzyme was activated by the action of little amount of trypsin and then hydrolyzed both substrates of Congo red-elastin and succinyl-L-trialanine p-nitroanilide. 3) The molecular weight of the inactive enzyme which was estimated by Sephadex G-75 gel filtration was a little larger than that of hog pancreatic elastase I. 4) The activated enzyme generated from the inactive elastase by the action of trypsin had remarkable resemblance of enzymochemical properties with hog pancreatic elastase I. It can therefore be presumed that the inactive latent elastase in the hog plasma is a proelastase-like enzyme but not be any complex forms of elastase with α_1-antitrypsin and/or α_2-macroglobulin, and is transferred from the hog pancreas into the blood.
公益社団法人日本薬学会の論文
1985-05-25