Evidence for two-domain subunit structure of kidney lipoate acetyltransferase
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چکیده
منابع مشابه
Evidence for two lipoic acid residues per lipoate acetyltransferase chain in the pyruvate dehydrogenase multienzyme complex of Escherichia coli.
The reaction of two maleimides, N-ethylmaleimide and bis-(N-maleimidomethyl) ether, with the pyruvate dehydrogenase multienzyme complex of Escherichia coli in the presence of the substrate, pyruvate, was examined. In both cases, the reaction was demonstrated to be almost exclusively with the lipoate acetyltransferase component, and evidence is presented to show that the most likely sites of rea...
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During the purification of mouse and human interferons, multiple active components have been detected. Mouse interferon was purified over 500-fold by differential precipitation, centrifugation, gel chromatography, and isoelectric focusing. On electrofocusing, two molecular forms (A and B) were noted. Form B (isoelectric point 7.35) had a molecular weight of about 38,000 and Form A (isoelectric ...
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Lipoate acetyltransferase (E2) forms the core of the pyruvate dehydrogenase multienzyme complex (reviewed [ 1,2]). The subunit Mr of mammalian E2 has been a matter of controversy. Using SDS-polyacrylamide gel electrophoresis Mr 74 000-76 000 has been found for the bovine as well as porcine kidney and heart enzyme [3-61. The same value was reported for pig heart E2 in a study employing gel filtr...
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متن کاملAmino acid sequence analysis of the lipoyl and peripheral subunit-binding domains in the lipoate acetyltransferase component of the pyruvate dehydrogenase complex from Bacillus stearothermophilus.
The pyruvate dehydrogenase multienzyme complex from Bacillus stearothermophilus comprises a structural core, composed of 60 dihydrolipoamide acetyltransferase (E2p) subunits, which binds multiple copies of pyruvate decarboxylase (E1p) and dihydrolipoamide dehydrogenase (E3) subunits. After limited proteolysis with chymotrypsin, the N-terminal lipoyl domain of E2p was excised, purified and seque...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1980
ISSN: 0014-5793
DOI: 10.1016/0014-5793(80)81156-2