THE PRESENCE OF ACYL-COA HYDROLASE IN RAT BROWN-ADIPOSE-TISSUE PEROXISOMES
THE PRESENCE OF ACYL-COA HYDROLASE IN RAT BROWN-ADIPOSE-TISSUE PEROXISOMES
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DOI：
10.1042/bj2620041
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发表时间：
1989-08-15
影响因子：
4.1
通讯作者：
BERGE, RK
中科院分区：
文献类型：
--
作者：
ALEXSON, SEH;OSMUNDSEN, H;BERGE, RK
研究了大鼠棕色脂肪组织中酰基辅酶A水解酶的亚细胞分布，特别强调可能的过氧化物酶体定位。蔗糖密度梯度离心的亚细胞分级分离，然后在NADH存在下测量短链（丙酰-CoA）酰基-CoA水解酶，导致在梯度中的两个活性峰：一个峰对应于细胞色素氧化酶（线粒体标记酶）的分布，另一个活性峰与过氧化物酶体标记酶过氧化氢酶相吻合。NADH抑制的短链水解酶活性的分布完全类似于细胞色素氧化酶。过氧化物酶体酰基辅酶A水解酶活性的底物特异性曲线表明存在表现出广泛底物特异性的单一酶，对链长为3-12个碳原子的脂肪酸具有最大活性。线粒体酰基-CoA水解酶活性被低浓度（μ M）的CoA和高浓度（> 0.8mM）的ATP抑制。与线粒体短链水解酶相比，过氧化物酶体酰基辅酶A水解酶活性不受NADH抑制。
The subcellular distribution of acyl-Coa hydrolase was studied in rat brown adipose tissue, with special emphasis on possible peroxisomal localization. Subcellular fractionation by sucrose-density-gradient centrifugation, followed by measurement of short-chain (propionyl-CoA) acyl-CoA hydrolase in the presence of NADH, resulted in two peaks of activity in the gradient: one peak corresponded to the distribution of cytochrome oxidase (mitochondrial marker enzyme),and another peak of activity coincided with the peroxisomal marker enzyme catalase. The distribution of the NADH-inhibited short-chain hydrolase activity fully resembled that of cytochrome oxidase. The substrate-specificity curve of the peroxisomal acyl-CoA hydrolase activity indicated the presence of a single enzyme exhibiting a broad substrate specificity, with maximal activity towards fatty acids with chain lengths of 3-12 carbon atoms. The mitochondrial acyl-CoA hydrolase activity was inhibited by CoA at low (.mu.M) concentrations and by ATP at high concentrations (> 0.8 mM). In contrast with the mitochondrial short-chain hydrolase, the peroxisomal acyl-CoA hydrolase activity was not inhibited by NADH.