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[莴苣叶片叶绿体碳酸酐酶的纯化与特性研究(作者译)]

[Purification and characterization of chloroplast carbonate dehydratase from leaves of Lactuca sativa (author's transl)].

作者信息

Walk R A, Metzner H

出版信息

Hoppe Seylers Z Physiol Chem. 1975 Nov;356(11):1733-41.

PMID:812792
Abstract

Two isoenzymes of carbonate dehydratase were identified in green leaf tissue of Lactuca sativa. Their molecular weights were found to be 195 000 and 250 000. The lighter isoenzyme (I) was further characterized. It is localized in the chloroplast fraction. With polyacrylamide gel electrophoresis in the presence of dodecyl sulphate, subunits with a molecular weight of 34 000 and higher aggregates of this size could be detected. This is interpreted as an indication of an hexameric enzyme structure. The 900-fold purified polymer contained 5 - 6 atoms of zinc. Amino acid composition and inhibition by acetazolamide (Diamox), cyanide, nitrate, azide and ferricyanide are described.

摘要

在莴苣的绿叶组织中鉴定出两种碳酸酐酶同工酶。发现它们的分子量分别为195000和250000。对较轻的同工酶(I)进行了进一步表征。它定位于叶绿体部分。在十二烷基硫酸盐存在下进行聚丙烯酰胺凝胶电泳时,可检测到分子量为34000的亚基以及这种大小的更高聚集体。这被解释为该酶具有六聚体结构的迹象。经过900倍纯化的聚合物含有5 - 6个锌原子。描述了其氨基酸组成以及乙酰唑胺(醋氮酰胺)、氰化物、硝酸盐、叠氮化物和铁氰化物对它的抑制作用。

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