Characterization of soybean trypsin inhibitor sensitive protease from unfertilized sea urchin eggs

Biochemistry ◽  
1985 ◽  
Vol 24 (15) ◽  
pp. 3926-3931 ◽  
Author(s):  
Mark C. Alliegro ◽  
Herbert Schuel
Keyword(s):  
Sea Urchin ◽  
Trypsin Inhibitor ◽  
Soybean Trypsin Inhibitor ◽  
Sea Urchin Eggs

Evidence that hatching enzyme of the sea urchin Strongylocentrotus purpuratus is a chymotrypsin-like protease

1988 ◽  
Vol 66 (11) ◽  
pp. 1200-1209 ◽  
Author(s):  
Laura L. Post ◽  
Regina Schuel ◽  
Herbert Schuel
Keyword(s):  
Ethyl Ester ◽  
Proteolytic Activity ◽  
Sea Urchin ◽  
Trypsin Inhibitor ◽  
Strongylocentrotus Purpuratus ◽  
Soybean Trypsin Inhibitor ◽  
Chloromethyl Ketone ◽  
Hatching Enzyme ◽  
Sea Urchin Eggs ◽  
Chymotrypsin Inhibitors

The sea urchin blastula secretes a hatching enzyme (HE) that dissolves the fertilization envelope. HE was collected from the supernatant seawater of cultures of hatched Strongylocentrotus purpuratus blastulae, and concentrated 20 times by ultrafiltration. The proteolytic activity of HE using casein as substrate was inhibited by the chymotrypsin inhibitors, chymostatin and N-tosyl-L-phenylalanine chloromethyl ketone. The activity was not inhibited by inhibitors (antipain, elastatinal, pepstatin, phosphoramidon, soybean trypsin inhibitor, and Nα-p-tosyl-L-lysine chloromethyl ketone) of other types of proteases. HE did not hydrolyze the synthetic trypsin substrate, α-N-benzoyl-L-arginine ethyl ester, but did hydrolyze the synthetic substrate of chymotrypsin, N-benzoyl-L-tyrosine ethyl ester (BTEE). The BTEEase activity of HE was completely inhibited by the chymotrypsin inhibitors chymostatin and 2-nitro-4-carboxyphenyl N,N-diphenylcarbamate (NCDC). Chymostatin inhibited the natural hatching of sea urchin blastulae. Application of HE to freshly fertilized sea urchin eggs, 2 h after insemination, caused premature dispersal of the hardened fertilization envelope. Chymostatin and NCDC inhibited HE-induced lysis of the fertilization envelope, while inhibitors of other types of proteases were ineffective. These data suggest that sea urchin HE is a chymotrypsin-like protease we call "chymostrypsin."

Characterization of Native Myosin VI Isolated from Sea Urchin Eggs

2007 ◽  
Vol 142 (4) ◽  
pp. 481-490 ◽  
Author(s):  
S. Sakata ◽  
Y. Watanabe ◽  
J. Usukura ◽  
I. Mabuchi
Keyword(s):  
Sea Urchin ◽  
Myosin Vi ◽  
Sea Urchin Eggs

Characterization of Anastral, Bipolar Spindle Development and Atypical Cytokinesis in Ammonia-Activated Sea Urchin Eggs

2004 ◽  
Vol 207 (2) ◽  
pp. 160-160
Author(s):  
John H. Henson ◽  
Jessica E. Davis ◽  
Charles B. Shuster ◽  
Christopher A. Fried ◽  
Calvin R. Simerly
Keyword(s):  
Sea Urchin ◽  
Bipolar Spindle ◽  
Sea Urchin Eggs ◽  
Spindle Development
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