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通过亲和色谱法纯化钴激活的酰基转移酶。

Purification of cobalt-activated acylase by affinity chromatography.

作者信息

Słowińska R, Szewczuk A

出版信息

Acta Biochim Pol. 1979;26(3):229-48.

PMID:573948
Abstract

alpha-Hydroxyisocaproyltyrosine (HyIc-Tyr-OH), a potent competitive inhibitor of the cobalt-activated acylase form 2, was synthesized. Its derivative, alpha-aminopentyl-HyIc-Tyr-OEt was coupled to cyanogen bromide-activated Sepharose 4B and was used for about 100-fold purification of the acylase from human liver by affinity chromatography. The preparation obtained did not show aminoacylase, aspartyl acylase or alanylarylamidase activities. The same chromatographic method was also applied to isolate form 2 of the serum acylase from patients with viral hepatitis and guinea pig placenta.

摘要

合成了α-羟基异己酰基酪氨酸(HyIc-Tyr-OH),它是钴激活的酰基转移酶形式2的一种有效竞争性抑制剂。其衍生物α-氨基戊基-HyIc-Tyr-OEt与溴化氰活化的琼脂糖4B偶联,并用于通过亲和色谱法从人肝脏中对酰基转移酶进行约100倍的纯化。所获得的制剂未显示出氨基酰基酶、天冬氨酰基酶或丙氨酰芳基酰胺酶活性。同样的色谱方法也被用于从病毒性肝炎患者和豚鼠胎盘中分离血清酰基转移酶形式2。

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