Trypsin-like hatching protease from mouse embryos: Evidence for the presence in culture medium and its enzymatic properties
✍ Scribed by Sawada, Hitoshi ;Yamazaki, Kimie ;Hoshi, Motonori
- Book ID
- 102893032
- Publisher
- John Wiley and Sons
- Year
- 1990
- Tongue
- English
- Weight
- 524 KB
- Volume
- 254
- Category
- Article
- ISSN
- 0022-104X
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✦ Synopsis
Abstract
Enzymatic properties of a protease involved in hatching of mouse embryos were examined. A trypsin‐like protease, which most efficiently hydrolyzed t‐butoxycarbonyl‐Leu‐Ser‐Thr‐Arg‐4‐methylcoumaryl‐7‐amide, was demonstrated in culture medium of mouse hatching embryos. The enzyme was strongly inhibited by diisopropyl fluorophosphate, phenylmethanesulfonyl fluoride, leupeptin, antipain, __N__α‐tosyl‐l‐lysyl‐chloromethane, soybean trypsin inhibitor, and Trasylol, but not or weakly inhibited by p‐chloromercuribenzoic acid, EDTA, E‐64, pepstain, chymostatin, and bestatin, suggesting a trypsin‐like serine proteinase. The protease activity in the medium gradually elevated during the course of hatching, whereas the embryo‐associated activity showed no significant change. Furthermore, pyroglutamyl‐Leu‐argininal, the strongest inhibitor for the enzyme among peptidyl argininals, all of which are potent trypsin inhibitors, showed the strongest inhibition toward hatching. Thus, a trypsin‐like protease secreted from hatching embryos into the culture medium may participate in mouse hatching, probably as a hatching enzyme.