Microheterogeneity of the glycoprotein subunit of the (sodium + potassium)-activated adenosine triphosphatase from the electroplax of Electrophorus electricus.
Microheterogeneity of the glycoprotein subunit of the (sodium + potassium)-activated adenosine triphosphatase from the electroplax of Electrophorus electricus.
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来自电电鱼电板的（钠钾）激活的腺苷三磷酸酶的糖蛋白亚基的微观异质性。
DOI：
10.1016/0006-291x(79)91820-5
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发表时间：
1979
影响因子：
3.1
通讯作者：
L. Hokin
中科院分区：
文献类型：
--
作者：
P. Marshall;L. Hokin
纯化的Na， k - atp酶在聚丙烯酰胺凝胶上的等电聚焦将蛋白质分解成十个条带。采用十二烷基硫酸钠凝胶过滤分离催化亚基和糖蛋白亚基。对分离的糖蛋白亚基进行等电聚焦，发现它占了10个条带中的9个。这种微异质性的部分原因可以归结为单个条带中唾液酸含量的变化，因为通过神经氨酸酶处理去除所有唾液酸使条带数量减少到4个。这表明糖蛋白亚基的微观异质性是由于在一个共同的多肽主链上的低聚糖的翻译后修饰。
Isoelectric focusing of purified Na,K-ATPase on polyacrylamide gels resolved the protein into ten bands. The catalytic and glycoprotein subunits were separated by sodium dodecyl sulfate gel filtration. Isoelectric focusing of the isolated glycoprotein subunit showed that it accounted for nine of the ten bands. Part of this microheterogeneity can be attributed to variations in sialic acid content in individual bands, since removal of all of the sialic acid by neuraminidase treatment reduced the number of bands to four. It is suggested that the microheterogeneity of the glycoprotein subunit is due to post-translational modifications of oligosaccharides on a common polypeptide backbone.