Purification of a Bovine Liver Protein Rapidly Phosphorylated by Adenosine Triphosphate

Autor:	Örjan Zetterqvist, Olov Wålinder, Lorentz Engström
Rok vydání:	1968
Předmět:	chemistry.chemical_classification Substrate (chemistry) Cell Biology Biology Biochemistry Molecular biology Hydrolysate chemistry.chemical_compound Enzyme chemistry biology.protein Phosphorylation Protein phosphorylation Protein G Molecular Biology Incubation Adenosine triphosphate
Zdroj:	Journal of Biological Chemistry. 243:2793-2798
ISSN:	0021-9258
Popis:	A bovine liver protein which is rapidly phosphorylated on incubation with AT32P has been highly purified. The molecular weight of the protein has been estimated to be approximately 100,000. Each protein molecule has been found to incorporate more than one phosphoryl group. From an alkaline hydrolysate of AT32P-incubated protein, 1-32P-phosphohistidine, 3-32P-phosphohistidine, and N-e-32P-phospholysine have been isolated. The possible role of the protein as an enzyme which is intermediately phosphorylated by its substrate is briefly discussed.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::0a883e527b7d3a6f6c4acf915b1c9c1e https://doi.org/10.1016/s0021-9258(18)93442-3 Zobrazit plný text záznamu