๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

A rapid assay for protein kinases phosphorylating small polypeptides and other substrates

โœ Scribed by S. Braun; M.Abdel Ghany; E. Racker


Publisher
Elsevier Science
Year
1983
Tongue
English
Weight
831 KB
Volume
135
Category
Article
ISSN
0003-2697

No coin nor oath required. For personal study only.

โœฆ Synopsis


A new and rapid method of protein kinase assay is presented which is suitable for low-molecular-weight substrates, irrespective of their electrophoretic or chromatographic mobility. It depends on the phosphorylation of the substrates with [gamma-32P]ATP, hydrolysis of the pyrophosphate bonds by boiling in 1 N HCl, extraction of 32P with isobutanol-benzene, and measurement of the radioactivity of 32P-labeled phosphoesters in the water phase. The method is shown to be suitable for both tyrosine- and serine-phosphorylating protein kinases.


๐Ÿ“œ SIMILAR VOLUMES


A rapid and sensitive assay method for p
โœ Kuo-Ping Huang; J.C. Robinson ๐Ÿ“‚ Article ๐Ÿ“… 1976 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 421 KB

A simplified assay method is described for the determination of protein kinase activity. Enzymatic activity is followed by measuring the incorporation of 32P from the terminal phosphoryl group of nucleoside triphosphates into protein substrate. Separation of the resulting 32P-labeled phosphoprotein

A tandem chromatographic column method f
โœ John J. Egan; Min-Kun Chang; Constantine Londos ๐Ÿ“‚ Article ๐Ÿ“… 1988 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 878 KB

A method was devised for assaying protein kinases that phosphorylate either Kemptide, such as cAMP-dependent protein kinase, or a glycogen synthase peptide, which is an excellent substrate for protein kinase C. Upon sequential processing of reaction mixtures through tandem columns of cation and anio

Gene cloning and utility phophorylation
โœ Kyong-Cheol Ko; Mi Hee Choi; Sang Hyun Park ๐Ÿ“‚ Article ๐Ÿ“… 2009 ๐Ÿ› John Wiley and Sons ๐ŸŒ French โš– 269 KB ๐Ÿ‘ 2 views

## Abstract The prototype of the cdc2 protein kinase in mammalian cells regulates its entry into mitosis by phosphorylating a group of key proteins in the major cell cycle transitions. In this study, using the mep45 gene encoding the 45โ€‰kDa major envelope protein (Mep45) of __Selenomonas ruminantiu