Partial purification and some properties of a neutral proteinase in rat ovary.
The ovary of rat possessed a neutral proteinase which had an optimum pH at around 8.5 in the presence of 0.5 M NaCl. The proteinase was soluble only in media of high ionic strength such as 2 M NaCl. In order to prevent the reprecipitation in media of low ionic strength of the enzyme solubilized, it is necessary to add protamine sulfate to the solubilizing medium. When the solubilized enzyme was applied to a Sephadex column, the proteinase activity was eluted at the same position as bovine alpha-chymotrypsinogen. The results using some protease inhibitors showed that the proteinase was a chymotrypsin-like serine enzyme. When rats were treated with compound 48/80, the proteinase activity almost completely disappeared, suggesting that the enzyme is of mast cell origin.
Laboratory of Biochemistry, Faculty of Environmental Health, Azabu University, Kanagawa, Japan.
M
M
Higuchi
F
F
Yoshida
D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D002919:Chymotrypsinogen / Q000302:isolation & purification; D003956:Dialysis; D005260:Female; D007700:Kinetics; D010053:Ovary / Q000201:enzymology*; D011480:Protease Inhibitors / Q000494:pharmacology; D051381:Rats; D017207:Rats, Sprague-Dawley; D012697:Serine Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism*
D011480:Protease Inhibitors; D002919:Chymotrypsinogen; D012697:Serine Endopeptidases