Activation of Rat Choline Acetyltransferase by Limited Proteolysis
نویسندگان
چکیده
منابع مشابه
Activation of rat liver microsomal glutathione transferase by limited proteolysis.
The activity of rat liver microsomal glutathione transferase is increased by limited tryptic proteolysis; the membrane-bound and purified forms of the enzyme are activated about 5- and 10-fold respectively. The cleavage sites that correlate with this activation were determined by amino acid sequence analysis to be located after Lys-4 and Lys-41. Differences in the relative extent of cleavage at...
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The localization, purification, and some enzymatic properties of choline acetyltransferase from rat brain were studied. Most assays were performed with a specific radiometric micromethod. Solubilization of the enzyme was examined after homogenization of cerebral cortices by means which disintegrate nerve endings. In isotonic KC1 the enzyme was recovered in solution. In more dilute KC1 the enzym...
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Four monoclonal antibodies were obtained to rat brain choline acetyltransferase (CAT). The enzyme was purified 95,000-fold from rat brain by precipitation with acetic acid at pH 4.5, fractionation with 40 to 60% (NH4)2SO4, CM-Sephadex chromatography, and affinity column chromatography on agarose-hexane-coenzyme A. The enzyme preparation was applied to the affinity column in the presence of 10 m...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1995
ISSN: 0021-9258
DOI: 10.1074/jbc.270.33.19395