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CORTEX PROTEIN OF SEA URCHIN EGGS I. ITS PURIFICATION AND OTHER PROTEIN COMPONENTS OF THE CORTEX
Author(s) -
MABUCHI ISSEI,
SAKAI HIKOICHI
Publication year - 1972
Publication title -
development, growth and differentiation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.864
H-Index - 66
eISSN - 1440-169X
pISSN - 0012-1592
DOI - 10.1111/j.1440-169x.1972.00247.x
Subject(s) - sea urchin , chemistry , cortex (anatomy) , tris , biochemistry , polyacrylamide gel electrophoresis , ultracentrifuge , chromatography , disulfide bond , cerebral cortex , biophysics , biology , microbiology and biotechnology , enzyme , neuroscience , endocrinology
Isolated cortical hull of the sea urchin egg consisted of a gel layer having 3–4 μ in thickness which could be dispersed with 0.6 m KCl. After removing a protein fraction soluble in 10 m m Tris‐HCl buffer (pH 7.0–7.2) containing 1 m m ATP or EDTA and 1 m m GSH, so called KCl‐soluble protein of the cortices was obtained. After purifying the “cortex protein”, it was homogeneous so far as checked by ultracentrifugation and electrophoresis on a polyacrylamide gel. The cortex protein had a thiol‐disulfide exchange activity to Ca‐insoluble protein in the ATP‐extract of the cortices catalyzed by a transhydrogenase. Neither ovoactin nor actomyosin‐like protein was detected in the ATP‐extract or the 0.6 m KCl‐extract of the cortices respectively. Hyalin was not detected in our KCl‐soluble protein fractions of isolated cortices.