酶促碘化的人唾液蛋白。通过柱色谱和等电聚焦进行分离和表征。
Enzymically iodinated human salivary proteins. Fractionation and characterization by column chromatography and electrofocusing.
作者信息
Sarimo S S, Tenovuo J
出版信息
Biochem J. 1977 Oct 1;167(1):23-9. doi: 10.1042/bj1670023.
Human salivary proteins were enzymically iodinated by the 125I-lactoperoxidase system. The proteins were than subjected to DEAE-cellulose column chromatography, preparative column electrofocusing and thin-layer polyacrylamide-gel electrofocusing. The radioactivity in the resolved protein pools and bands was determined. Results show that salivary proteins differ in their susceptibility to iodination carried out by this enzymic method. Two major iodine-binding protein fractions were discovered: one behaved like serum albumin on electrofocusing and was most susceptible to iodination by lactoperoxidase, and other had pI characteristics similar to those of salivary amylase. The physiological significance of the iodination of salivary proteins, which can also take place in vivo, is discussed.
人唾液蛋白通过¹²⁵I-乳过氧化物酶系统进行酶促碘化。然后将这些蛋白质进行DEAE-纤维素柱层析、制备性柱电聚焦和薄层聚丙烯酰胺凝胶电聚焦。测定了分离出的蛋白质池和条带中的放射性。结果表明，唾液蛋白对这种酶促碘化方法的敏感性不同。发现了两个主要的碘结合蛋白组分：一个在电聚焦时表现得像血清白蛋白，对乳过氧化物酶碘化最敏感，另一个的pI特征与唾液淀粉酶相似。还讨论了唾液蛋白碘化在体内也会发生的生理意义。
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