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Chymotrypsin-like and trypsin-like protease activities in the sea urchin (Hemicentrotus pulcherrimus) egg.
Experientia. 1992 Mar 15; 48(3):287-90.E

Abstract

Proteolytic activities in extracts of sea urchin eggs were examined using SDS (sodium dodecyl sulphate)-polyacrylamide gels. In the unfertilized eggs, proteases were detected as bands corresponding to the molecular weights of 40 kD and 26 kD on the gelatin gel, and 35 kD and 30 kD on the casein gel. Using various protease inhibitors, it was found that 40 kD, 30 kD, and 26 kD are chymotrypsin-like proteases and that 35 kD is a trypsin-like protease. The activity of the 40 kD chymotrypsin-like protease was found to be almost completely lost after insemination.

Authors+Show Affiliations

Taniguchi Y
Zoological Institute, Faculty of Science, University of Tokyo, Japan.

MeSH

AnimalsChymotrypsinElectrophoresis, Polyacrylamide GelOvumSea UrchinsSubstrate SpecificityTrypsinTrypsin Inhibitors

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

1547864

Citation

Taniguchi, Y. "Chymotrypsin-like and Trypsin-like Protease Activities in the Sea Urchin (Hemicentrotus Pulcherrimus) Egg." Experientia, vol. 48, no. 3, 1992, pp. 287-90.
Taniguchi Y. Chymotrypsin-like and trypsin-like protease activities in the sea urchin (Hemicentrotus pulcherrimus) egg. Experientia. 1992;48(3):287-90.
Taniguchi, Y. (1992). Chymotrypsin-like and trypsin-like protease activities in the sea urchin (Hemicentrotus pulcherrimus) egg. Experientia, 48(3), 287-90.
Taniguchi Y. Chymotrypsin-like and Trypsin-like Protease Activities in the Sea Urchin (Hemicentrotus Pulcherrimus) Egg. Experientia. 1992 Mar 15;48(3):287-90. PubMed PMID: 1547864.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Chymotrypsin-like and trypsin-like protease activities in the sea urchin (Hemicentrotus pulcherrimus) egg. A1 - Taniguchi,Y, PY - 1992/3/15/pubmed PY - 1992/3/15/medline PY - 1992/3/15/entrez SP - 287 EP - 90 JF - Experientia JO - Experientia VL - 48 IS - 3 N2 - Proteolytic activities in extracts of sea urchin eggs were examined using SDS (sodium dodecyl sulphate)-polyacrylamide gels. In the unfertilized eggs, proteases were detected as bands corresponding to the molecular weights of 40 kD and 26 kD on the gelatin gel, and 35 kD and 30 kD on the casein gel. Using various protease inhibitors, it was found that 40 kD, 30 kD, and 26 kD are chymotrypsin-like proteases and that 35 kD is a trypsin-like protease. The activity of the 40 kD chymotrypsin-like protease was found to be almost completely lost after insemination. SN - 0014-4754 UR - https://www.unboundmedicine.com/medline/citation/1547864/Chymotrypsin_like_and_trypsin_like_protease_activities_in_the_sea_urchin__Hemicentrotus_pulcherrimus__egg_ DB - PRIME DP - Unbound Medicine ER -