Characterization of rat brain microsomal acyl-coenzyme A ligases: different enzymes for the synthesis of palmitoyl-coenzyme A and lignoceroyl-coenzyme A.
Characterization of rat brain microsomal acyl-coenzyme A ligases: different enzymes for the synthesis of palmitoyl-coenzyme A and lignoceroyl-coenzyme A.
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大鼠脑微粒体酰基辅酶 A 连接酶的表征:用于合成棕榈酰辅酶 A 和木脂酰辅酶 A 的不同酶。
DOI:
10.1016/0003-9861(86)90482-0
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发表时间:
1986
影响因子:
3.9
通讯作者:
Singh,I
中科院分区:
文献类型:
--
作者:
Bhushan,A;Singh,RP;Singh,I
Palmitic acid solubilized with Triton WR-1339 was converted to palmitoyl-CoA by microsomal membranes but lignoceric acid solubilized with Triton WR-1339 was not an effective substrate even though the detergent dispersed the same amount of these fatty acids and was also not inhibitory to the enzyme [I. Singh, RP Singh, A. Bhushan, and AK Singh (1985) Arch. Biochem. Biophys. 236, 418–426]. This observation suggested that palmitoyl-CoA and lignoceroyl-CoA may be synthesized by two different enzymes. We have solubilized the acyl-CoA ligase activities for palmitic and lignoceric acid of rat brain microsomal membranes with Triton X-100 and resolved them into three separate peaks (fractions) by hydroxylapatite chromatography. Fraction A (palmitoyl-CoA ligase) had high specific activity for palmitic acid and Fraction C (lignoceroyl-CoA ligase) for lignoceric acid. Specific activity of palmitoyl-CoA ligase for palmitic acid was six times higher than in Fraction C and specific activity of lignoceroyl-CoA ligase for lignoceric acid was four times higher than in Fraction A. At higher concentrations of Triton X-100 (0.5%), lignoceroyl-CoA ligase loses activity whereas palmitoyl-CoA ligase does not. Lignoceroyl-CoA ligase lost 60% of activity at 0.6% Triton X-100. Palmitoyl-CoA ligase (T 1 2 of 4.5 min) is more stable at 40° C than lignoceroyl-CoA ligase (T 1 2 of 1.5 min). The pH optimum of palmitoyl-CoA ligase was 7.7 and that of lignoceroyl-CoA ligase was 8.4. Similar to our results with intact membranes, palmitic acid solubilized with Triton WR-1339 was converted to palmitoyl-CoA by palmitoyl-CoA ligase whereas lignoceric acid when solubilized with Triton WR-1339 was not able to act as substrate for lignoceroyl-CoA ligase. Since solubilized enzyme activities for synthesis of palmitoyl-CoA and lignoceroyl-CoA from microsomal membranes can be resolved into different fractions by column chromatography and demonstrate different properties, we suggest that in microsomal membranes palmitoyl-CoA and lignoceroyl-CoA are synthesized by two different enzymes.
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DOI:
--
发表时间:
1971
期刊:
Biochimica et Biophysica Acta
影响因子:
--
作者:
Magne Aas
通讯作者:
Magne Aas
DOI:
--
发表时间:
1982
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
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通讯作者:
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DOI:
--
发表时间:
1968
期刊:
Biochimica et Biophysica Acta
影响因子:
--
作者:
S. Pande;J. Mead
通讯作者:
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影响因子:
3.9
作者:
I. Singh;R. Singh;A. Bhushan;A. K. Singh
通讯作者:
A. K. Singh
DOI:
--
发表时间:
1975
期刊:
Biochimica et Biophysica Acta
影响因子:
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作者:
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