来自嗜热栖热菌的膜相关蛋白丝氨酸/苏氨酸激酶是一种糖蛋白。
The membrane-associated protein-serine/threonine kinase from Sulfolobus solfataricus is a glycoprotein.
作者信息
Lower Brian H, Kennelly Peter J
机构信息
Department of Biochemistry-0308, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061, USA.
出版信息
J Bacteriol. 2002 May;184(10):2614-9. doi: 10.1128/JB.184.10.2614-2619.2002.
Abstract
Treatment of a sodium dodecyl sulfate-polyacrylamide gel with periodic acid-Schiff (PAS) stain or blotting with Galanthus nivalis agglutinin revealed the presence of several glycosylated polypeptides in a partially purified detergent extract of the membrane fraction of Sulfolobus solfataricus. One of the glycoproteins comigrated with the membrane-associated protein-serine/threonine kinase from S. solfataricus, which had been radiolabeled by autophosphorylation with [(32)P]ATP in vitro. Treatment with a chemical deglycosylating agent, trifluoromethanesulfonic acid, abolished PAS staining and reduced the M(r) of the protein kinase from approximately 67,000 to approximately 62,000. Protein kinase activity also adhered to, and could be eluted from, agarose beads containing bound G. nivalis agglutinin. Glycosylation of the protein kinase implies that at least a portion of this integral membrane protein resides on the external surface of the cell membrane.
摘要
用高碘酸-希夫（PAS）染色法处理十二烷基硫酸钠-聚丙烯酰胺凝胶，或用雪花莲凝集素进行印迹分析，结果显示，在嗜热栖热菌膜组分的部分纯化去污剂提取物中存在几种糖基化多肽。其中一种糖蛋白与嗜热栖热菌的膜相关蛋白-丝氨酸/苏氨酸激酶迁移率相同，该激酶已在体外通过用[（32）P]ATP进行自磷酸化而被放射性标记。用化学去糖基化剂三氟甲磺酸处理后，PAS染色消失，蛋白激酶的相对分子质量（Mr）从约67,000降至约62,000。蛋白激酶活性也附着于含有结合的雪花莲凝集素的琼脂糖珠上，并可从其上洗脱下来。蛋白激酶的糖基化表明，这种整合膜蛋白至少有一部分位于细胞膜的外表面。
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