The Membrane-Associated Protein-Serine/Threonine Kinase from Sulfolobus solfataricus Is a Glycoprotein
作者： Brian H. Lower , Peter J. Kennelly
DOI: 10.1128/JB.184.10.2614-2619.2002
关键词: Autophosphorylation 、 Biology 、 Protein kinase A 、 c-Raf 、 Protein kinase C 、 MAP2K7 、 Serine/threonine-specific protein kinase 、 Molecular biology 、 Biochemistry 、 Receptor protein serine/threonine kinase 、 Sulfolobus solfataricus
摘要: Treatment of a sodium dodecyl sulfate-polyacrylamide gel with periodic acid-Schiff (PAS) stain or blotting Galanthus nivalis agglutinin revealed the presence several glycosylated polypeptides in partially purified detergent extract membrane fraction Sulfolobus solfataricus. One glycoproteins comigrated membrane-associated protein-serine/threonine kinase from S. solfataricus, which had been radiolabeled by autophosphorylation [32P]ATP vitro. chemical deglycosylating agent, trifluoromethanesulfonic acid, abolished PAS staining and reduced Mr protein ∼67,000 to ∼62,000. Protein activity also adhered to, could be eluted from, agarose beads containing bound G. agglutinin. Glycosylation implies that at least portion this integral resides on external surface cell membrane.
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