Isolation and characterization of (Na,K)-ATPase proteolipid.
Isolation and characterization of (Na,K)-ATPase proteolipid.
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DOI：
10.1016/s0006-291x(80)80080-5
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发表时间：
1980-08
影响因子：
3.1
通讯作者：
Anita S. Reeves;Anita S. Reeves;John H. Collins;Arnold Schwartz
中科院分区：
文献类型：
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作者：
Anita S. Reeves;Anita S. Reeves;John H. Collins;Arnold Schwartz
从羔羊肾（Na，K）-ATP酶中，经SepharoseCL-6 B柱层析，氯仿-甲醇抽提，SephadexLH-60柱层析，分离出Mr为12，000的两种蛋白脂组分（γ_1和γ_2）。平均回收率为0.6 mol γ1和0.3 mol γ2/mol回收的催化亚基，表明蛋白脂以化学计量的量存在于酶中。γ1和γ2具有相似的氨基酸组成，其中γ1在疏水性氨基酸中较高，在带电氨基酸中较低。这两种组分都类似于从牛心（Na，K）-ATPase中分离的Mr为11，700的磷酸化蛋白。
We have isolated two proteolipid components (γ1 and γ2) of Mr∼ 12,000 from highly purified lamb kidney (Na,K)-ATPase by chromatography of the enzyme of Sepharose CL-6B, followed by extraction with a chloroform: methanol solvent and chromatography on Sephadex LH-60. The average recoveries are 0.6 mol of γ1 and 0.3 mol of γ2 per mol of catalytic subunit recovered, suggesting that proteolipid is present in stoichiometric amounts in the enzyme. γ1 and γ2 have similar amino acid compositions, with γ1 being higher in hydrophobic amino acids and lower in charged amino acids. Both components are similar to a Mr∼ 11,700 phosphorylated protein isolated from beef heart (Na,K)-ATPase.