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Purification of Acetylcholinesterase from Sea Urchin ( Hemicentrotus pulcherrimus ) Embryos by Affinity Chromatography
Author(s) -
AKASAKA KOJI,
SASAKI HIROSHI,
SHIMADA HIRAKU,
SHIROYA TSUGIO
Publication year - 1986
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.1986.00085.x
Subject(s) - hemicentrotus , acetylcholinesterase , sea urchin , affinity chromatography , chemistry , embryo , aché , enzyme , gastrulation , sepharose , yield (engineering) , chromatography , biochemistry , biology , microbiology and biotechnology , embryogenesis , materials science , metallurgy
Only one form of acetylcholinesterase (AchE) was detected in Hemicentrotus pulcherrimus embryos. In H. pulcherrimus embryos as well as in the other sea urchin embryos, AchE activity begins to increase rapidly after gastrula stage. Purification of AchE from plutei has been carried out by the procedure including affinity chromatography. Purified AchE had the activity 14,600 times higher than that of homogenate, and the final yield of AchE was 8%. The enzyme seems to be electrophoretically homogeneous, and has a molecular weight of 3 × 10 5 as determined by Sepharose CL–6B column chromatography.