脯氨酰羟化酶存在内源性抑制作用的证据。

Evidence for the presence of an endogenous inhibition of prolyl hydroxylase.

作者信息

Chichester C O, Fuller G C

出版信息

Res Commun Chem Pathol Pharmacol. 1980 Aug;29(2):329-38.

Abstract

Prolyl hydroxylase [EC 1.14.11.2] was shown to be inhibited by an ultrafiltrate (less than 30,000 molecular weight) fraction isolated from skin and blood of neonatal and adult rabbits. This fraction also inhibited two other alpha-ketoglutarate requiring mixed function oxidases, lysyl hydroxylase [EC 1.14.11.4] and alpha-butyrobetaine hydroxylase [EC 1.14.11.1] but not the amine oxidase, lysyl oxidase. Purification of the skin ultrafiltrate on Sephadex G-25 demonstrated a peak of prolyl hydroxylase inhibitory activity which chromatographed at a molecular weight corresponding to approximately 3,000. Chromatography of a blood ultrafiltrate separated a similar peak of material which was inhibitory for prolyl hydroxylase.

摘要

脯氨酰羟化酶[EC 1.14.11.2]被证明受到从新生和成年兔的皮肤及血液中分离出的超滤部分（分子量小于30,000）的抑制。该部分还抑制另外两种需要α-酮戊二酸的混合功能氧化酶，即赖氨酰羟化酶[EC 1.14.11.4]和α-丁甜菜碱羟化酶[EC 1.14.11.1]，但不抑制胺氧化酶赖氨酰氧化酶。在葡聚糖凝胶G-25上对皮肤超滤物进行纯化，显示出脯氨酰羟化酶抑制活性的一个峰值，其色谱分离时的分子量约为3000。对血液超滤物进行色谱分析，分离出了一个类似的对脯氨酰羟化酶有抑制作用的物质峰值。

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