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与碳酸酐酶同工酶相关的色谱法和电泳法。

Chromatographic and electrophoretic methods related to the carbonic anhydrase isozymes.

作者信息

Bergenhem N

机构信息

Department of Biological Chemistry, University of Michigan, Abn Arbor 48109-2007, USA.

出版信息

J Chromatogr B Biomed Appl. 1996 Sep 20;684(1-2):289-305. doi: 10.1016/0378-4347(95)00566-8.

DOI:10.1016/0378-4347(95)00566-8
PMID:8906478
Abstract

There are three gene families that encode zinc metalloenzymes that catalyze the reversible hydration of CO2. The encoded enzymes are termed carbonic anhydrases (CAs). The CA isozymes have been purified from representatives of all types of organisms. Most CAs are strongly inhibited by aromatic sulfonamides. Several chromatographic and electrophoretic methods have been devised to determine binding constants for sulfonamides to CAs, and these compounds have been extensively used for, often single-step, affinity chromatographic separation of CAs from complex matrixes. The purification of different CA isozymes from different organisms is reviewed, as are methods for detection of CAs during chromatography and electrophoresis.

摘要

有三个基因家族编码催化二氧化碳可逆水合反应的锌金属酶。所编码的酶被称为碳酸酐酶(CAs)。碳酸酐酶同工酶已从所有类型生物体的代表中纯化出来。大多数碳酸酐酶受到芳香族磺酰胺的强烈抑制。已经设计了几种色谱和电泳方法来测定磺酰胺与碳酸酐酶的结合常数,并且这些化合物已广泛用于(通常是单步)从复杂基质中亲和色谱分离碳酸酐酶。本文综述了从不同生物体中纯化不同碳酸酐酶同工酶的方法,以及在色谱和电泳过程中检测碳酸酐酶的方法。

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