1985 年 105 巻 5 号 p. 499-506
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 α1-antitrypsin and/or α2-macroglobulin, and is transferred from the hog pancreas into the blood.