Ascidian sperm chymotrypsin-like enzyme; participation in fertilization
- 1 April 1983
- journal article
- research article
- Published by Springer Science and Business Media LLC in Cellular and Molecular Life Sciences
- Vol. 39 (4), 377-378
- https://doi.org/10.1007/bf01963132
Abstract
The action of a chymotrypsin-like enzyme from sperm extract from the ascidianHalocynthia roretzi was studied using several substrates. It was found that the most susceptible substrate had the most powerful inhibitory effect on fertilization in this animal. Among the substrates, the order of susceptibility coincided with the order of inhibitory ability, which indicates that the enzyme is involved in the fertilization process.Keywords
This publication has 13 references indexed in Scilit:
- Purification and Characterization of a Chymotrypsin‐Like Enzyme from Sperm of the Sea Urchin, Hemicentrotus puleherrimusEuropean Journal of Biochemistry, 1982
- Properties of the vitelline coat lysin from toad spermJournal of Experimental Zoology, 1982
- Evidence for acrosin‐like enzyme in sperm extract and its involvement in fertilization of the ascidian, halocynthia roretziGamete Research, 1982
- Involvement of trypsin-like activity in binding of mouse spermatozoa to zonae pellucidae.Proceedings of the National Academy of Sciences, 1981
- Evidence for participation of sperm proteinases in fertilization of the solitary ascidian, Halocynthia roretzi: Effects of protease inhibitorsDevelopmental Biology, 1981
- Periodic spawning of three types of the ascidian,Halocynthia roretzi (Drasche), under continuous light conditionsJournal of Experimental Zoology, 1980
- A study of the chorion and the follicle cells in relation to the sperm-egg interaction in the ascidian, Ciona intestinalisDevelopmental Biology, 1980
- Effects of hydrolase inhibitors on fertilization of sea urchins: I. Protease inhibitorsGamete Research, 1979
- Biochemistry of Mammalian FertilizationAnnual Review of Biochemistry, 1974
- On the size of the active site in proteases. I. PapainBiochemical and Biophysical Research Communications, 1967