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前列腺素的生物合成

Biosynthesis of prostaglandins.

作者信息

Hemler M E, Lands W E

出版信息

Lipids. 1977 Jul;12(7):591-5. doi: 10.1007/BF02533387.

DOI:10.1007/BF02533387
PMID:408576
Abstract

Highly purified cyclooxygenase from sheep vesicular glands is stimulated by the presence of protoporphyrin IX compounds. This stimulation may be due to the conversion of an apoenzyme to the holoenzyme, and full activity is achieved when half of the enzyme subunits (70,000 daltons) bind heme. Also, one-half of the subunits appear to contain non-heme iron. The apparent molecular weight of the holoenzyme is approximately 300,000 daltons and is compatible with a complex of four 70,000 dalton subunits. Thus, we suggest that heme and non-heme iron may be attached to different 70,000 daltons subunits that make up an A2B2-type of peptide chain arrangement.

摘要

来自绵羊精囊的高度纯化的环氧化酶受到原卟啉IX化合物的刺激。这种刺激可能是由于脱辅基酶转变为全酶,当一半的酶亚基(70,000道尔顿)结合血红素时可达到完全活性。此外,一半的亚基似乎含有非血红素铁。全酶的表观分子量约为300,000道尔顿,与四个70,000道尔顿亚基组成的复合物相符。因此,我们认为血红素和非血红素铁可能附着于构成A2B2型肽链排列的不同70,000道尔顿亚基上。

相似文献

1
Biosynthesis of prostaglandins.前列腺素的生物合成
Lipids. 1977 Jul;12(7):591-5. doi: 10.1007/BF02533387.
2
Properties of solubilized prostaglandin synthetase from sheep vesicular glands.绵羊精囊可溶性前列腺素合成酶的特性
Life Sci. 1975 Sep 15;17(6):951-8. doi: 10.1016/0024-3205(75)90448-8.
3
Purification of the cyclooxygenase that forms prostaglandins. Demonstration of two forms of iron in the holoenzyme.形成前列腺素的环氧化酶的纯化。全酶中两种形式铁的证明。
J Biol Chem. 1976 Sep 25;251(18):5575-9.
4
Proceedings: Properties of solubilized prostaglandin synthetase from sheep vesicular glands.论文集:绵羊精囊可溶性前列腺素合成酶的特性
Isr J Med Sci. 1975 Nov;11(11):1178.
5
Purification and characterisation of prostaglandin endoperoxide synthetase from sheep vesicular glands.绵羊精囊前列腺素内过氧化物合成酶的纯化与特性分析
Biochim Biophys Acta. 1977 May 25;487(2):315-31. doi: 10.1016/0005-2760(77)90008-x.
6
Purification of prostaglandin endoperoxide synthetase from bovine vesicular gland microsomes.从牛精囊微粒体中纯化前列腺素内过氧化物合成酶。
J Biol Chem. 1976 May 10;251(9):2629-36.
7
Properties of a partially-purified preparation of the prostaglandin-forming oxygenase from sheep vesicular gland.绵羊精囊前列腺素合成加氧酶部分纯化制剂的性质
Prostaglandins. 1975 Nov;10(5):813-24. doi: 10.1016/0090-6980(75)90010-6.
8
Mechanism for suppression of cellular biosynthesis of prostaglandins.抑制前列腺素细胞生物合成的机制。
Nature. 1976 Apr 15;260(5552):630-2. doi: 10.1038/260630a0.
9
Prostaglandin H synthase. Stoichiometry of heme cofactor.
J Biol Chem. 1984 May 25;259(10):6358-63.
10
The heme-binding properties of prostaglandin synthetase from sheep vesicular gland.绵羊精囊前列腺素合成酶的血红素结合特性。
J Biol Chem. 1981 Oct 10;256(19):10018-22.

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本文引用的文献

1
Protein measurement with the Folin phenol reagent.使用福林酚试剂进行蛋白质测定。
J Biol Chem. 1951 Nov;193(1):265-75.
2
Cofactor requirements of the enzyme synthesizing prostagland in bovine seminal vesicles.牛精囊腺中前列腺素合成酶的辅助因子需求
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Oxygenation of polyunsaturated fatty acids during prostaglandin biosynthesis by sheep vesicular gland.绵羊精囊在前列腺素生物合成过程中多不饱和脂肪酸的氧化作用。
前列腺素F2α(PGF2α):伤口活力的一个不充分指标?
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Purification and properties of rat liver tryptophan oxygenase.大鼠肝脏色氨酸加氧酶的纯化及性质
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5
Soyabean lipoxygenase: an iron-containing enzyme.大豆脂氧合酶:一种含铁酶。
Biochim Biophys Acta. 1973 Nov 15;327(1):24-31. doi: 10.1016/0005-2744(73)90099-5.
6
Evidence for an activating factor formed during prostaglandin biosynthesis.前列腺素生物合成过程中形成激活因子的证据。
Biochem Biophys Res Commun. 1975 Jul 22;65(2):464-71. doi: 10.1016/s0006-291x(75)80170-7.
7
Purification of the cyclooxygenase that forms prostaglandins. Demonstration of two forms of iron in the holoenzyme.形成前列腺素的环氧化酶的纯化。全酶中两种形式铁的证明。
J Biol Chem. 1976 Sep 25;251(18):5575-9.
8
Mechanism for suppression of cellular biosynthesis of prostaglandins.抑制前列腺素细胞生物合成的机制。
Nature. 1976 Apr 15;260(5552):630-2. doi: 10.1038/260630a0.
9
Purification of prostaglandin endoperoxide synthetase from bovine vesicular gland microsomes.从牛精囊微粒体中纯化前列腺素内过氧化物合成酶。
J Biol Chem. 1976 May 10;251(9):2629-36.
10
Properties of a partially-purified preparation of the prostaglandin-forming oxygenase from sheep vesicular gland.绵羊精囊前列腺素合成加氧酶部分纯化制剂的性质
Prostaglandins. 1975 Nov;10(5):813-24. doi: 10.1016/0090-6980(75)90010-6.