Purification and properties of human D-3-hydroxyacyl-CoA dehydratase: medium-chain enoyl-CoA hydratase is D-3-hydroxyacyl-CoA dehydratase.
Purification and properties of human D-3-hydroxyacyl-CoA dehydratase: medium-chain enoyl-CoA hydratase is D-3-hydroxyacyl-CoA dehydratase.
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人D-3-羟酰基-CoA脱水酶的纯化和性质：中链烯酰基-CoA水合酶是D-3-羟酰基-CoA脱水酶。
DOI：
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发表时间：
1996
期刊：
影响因子：
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通讯作者：
T. Hashimoto
中科院分区：
文献类型：
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作者：
L. L. Jiang;A. Kobayashi;H. Matsuura;H. Fukushima;T. Hashimoto
从肝脏中纯化人中链烯酰辅酶A水合酶，因为我们注意到在人皮肤成纤维细胞中存在高的中链烯酰辅酶A水合酶活性，该酶由不同于催化烯酰辅酶A水合酶反应的已知酶的酶催化。获得两种酶制剂。其中之一，制剂I，由46 kDa的多肽，其分子量估计为86 kDa。另一种是制备物II，由主要的77-kDa多肽和次要的较小多肽（包括46-kDa多肽）组成。制剂II的分子量为154 kDa。两种酶制剂催化中链D-3-羟酰基-CoA可逆脱水为2-反式-烯酰基-CoA，但不与L-3-羟酰基-CoA反应。这些酶制剂的催化性质和免疫化学反应性几乎相同。通过对培养的人皮肤成纤维细胞的免疫组织化学研究，证实与抗体交叉反应的物质存在于过氧化物酶体中。
Human medium-chain enoyl-CoA hydratase was purified from liver, because we noticed the presence of a high medium-chain enoyl-CoA hydratase activity in human skin fibroblasts catalyzed by an enzyme different from the known enzymes catalyzing the enoyl-CoA hydratase reaction. Two enzyme preparations were obtained. One of them, preparation I, consisted of 46-kDa polypeptide, and its molecular mass was estimated to be 86 kDa. The other, preparation II, consisted of a major 77-kDa polypeptide and minor smaller polypeptides including 46-kDa polypeptide. The molecular mass of preparation II was 154 kDa. Both enzyme preparations catalyzed reversible dehydration of medium-chain D-3-hydroxyacyl-CoA to 2-trans-enoyl-CoA, but did not react with L-3-hydroxyacyl-CoA. Catalytic properties and immunochemical reactivities of these enzyme preparations were nearly the same. The cross-reactive material to the antibody was confirmed to be in peroxisomes by immunohistochemical study of cultured human skin fibroblasts.
来自大鼠肝脏过氧化物酶体的 D-3-羟酰辅酶 A 脱水酶。
DOI：
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发表时间：
1990
期刊：
The Journal of biological chemistry
影响因子：
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作者：
Li,JX;Smeland,TE;Schulz,H
通讯作者：
Schulz,H
从大鼠肝微粒体中纯化的 β-羟酰基-CoA 脱水酶具有过氧化物酶体来源的证据。
DOI：
10.1042/bj2870091
发表时间：
1992
期刊：
The Biochemical journal
影响因子：
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作者：
Cook,L;Nagi,MN;Suneja,SK;Hand,AR;Cinti,DL
通讯作者：
Cinti,DL