Wistrand P J, Wåhlstrand T
Biochim Biophys Acta. 1977 Apr 12;481(2):712-21. doi: 10.1016/0005-2744(77)90305-9.
Rat renal and erythrocyte carbonic anhydrases (carbonate hydro-lyase, EC 4.2.1.1) were isolated by affinity chromatography. The erythrocytes contain two major forms of the enzyme. One of the forms has a specific activity (towards CO2) 30 times higher than the other and constitutes the major part of the total cellular carbonic anhydrase. The amino acid compositions of this high-activity type and of the low-activity type are similar to the compositions reported for these types in other species. The kidney appears to have only one high-activity form of carbonic anhydrase which is very similar to and probably identical with the erythrocyte high-activity form.
通过亲和层析法分离出大鼠肾和红细胞碳酸酐酶(碳酸水解酶,EC 4.2.1.1)。红细胞含有两种主要形式的该酶。其中一种形式的酶(对CO2的)比活性比另一种高30倍,并且构成了细胞总碳酸酐酶的主要部分。这种高活性类型和低活性类型的氨基酸组成与其他物种中报道的这些类型的组成相似。肾脏似乎只有一种高活性形式的碳酸酐酶,它与红细胞高活性形式非常相似,可能是相同的。