Hydrodynamic properties of the sucrase-isomaltase complex from rabbit small intestine.
Hydrodynamic properties of the sucrase-isomaltase complex from rabbit small intestine.
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兔小肠蔗糖酶-异麦芽糖酶复合物的流体动力学特性。
DOI：
10.1111/j.1432-1033.1973.tb02934.x
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发表时间：
1973
期刊：
影响因子：
--
通讯作者：
H. Sund
中科院分区：
文献类型：
--
作者：
H. Mosimann;G. Semenza;H. Sund
1
根据蔗糖酶·异麦芽糖酶复合物在低离子强度下的流体动力学性质，计算出分子量为221000。络合物在高离子强度下二聚。
2
在变性条件下，复合物解离成两个分子量相同或几乎相同（112000）的亚基，推测它们各由一条多肽链组成。
3
异麦芽糖酶亚基以酶活性形式分离，分子量为113000。
1
From the hydrodynamic properties of the sucrase · isomaltase complex at low ionic strength, a molecular weight of 221000 was calculated. The complex dimerizes at high ionic strength.
2
Under denaturing conditions the complex dissociates into two subunits of identical or almost identical molecular weight (112000) which are presumably composed of one polypeptide chain each.
3
The isomaltase subunit, isolated in enzymatically active form, has a molecular weight of 113000.