Partial characterization of a nuclear proteolytic activity from fertilized sea urchin eggs.
The nuclei from fertilized sea urchin eggs, obtained 80 min after fertilization, contains a neutral proteolytic activity. Optimal action on casein was observed at pH 7-8 and a Km value of 1.2 mg/ml was determined for this substrate. The proteolytic activity was stimulated 1.5 fold by the addition of 3 M urea and decreased at higher urea concentrations. NaCl and CaCl2 were inhibitory whereas MgCl2 increased the enzyme activity. Isolated histones from sea urchin sperms, and especially histones H1, H2A, H2B and H3, were degraded by the nuclear activity. A partial inhibition of histones degradation was caused by sodium bisulfite and NaCl. The proteolytic activity was found associated to the chromatin of fertilized sea urchin eggs.
Sanchez-Chiang
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Departamento de Biologia Molecular, Facultad de Ciencias Biológicas y de Recursos Naturales, Universidad de Concepción, Chile.
Contreras
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Ainol
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D000818:Animals; D002467:Cell Nucleus / Q000201:enzymology*; D002843:Chromatin / Q000201:enzymology; D005260:Female; D006657:Histones / Q000378:metabolism; D007700:Kinetics; D010447:Peptide Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D012617:Sea Urchins; D013379:Substrate Specificity; D015053:Zygote / Q000201:enzymology*
D002843:Chromatin; D006657:Histones; D010447:Peptide Hydrolases