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001-es BibID:	BIBFORM001046
Első szerző:	Hlavanda Emma
Cím:	Phosphorylation blocks the activity of tubulin polymerization-promoting protein (TPPP) : identification of sites targeted by different kinases / Emma Hlavanda, Eva Klement, Endre Kókai, János Kovács, Orsolya Vincze, Natália Tőkési, Ferenc Orosz, Katalin F. Medzihradszky, Viktor Dombrádi, Judit Ovádi
Dátum:	2007
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban ERK2 PKA Cdk5 mass spectrometry
Megjelenés:	The Journal of Biological Chemistry 282 : 40 (2007), p. 29531-29539. -
További szerzők:	Klement Éva Kókai Endre (1971-) (biokémikus, biológus) Kovács János (orvos) Vincze Orsolya (orvos) Tőkési Natália Orosz Ferenc Medzihradszky-Fölkl Katalin Dombrádi Viktor (1953-) (biokémikus) Ovádi Judit
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001-es BibID:	BIBFORM028263
Első szerző:	Silberman, Steven R.
Cím:	Isolation and characterization of rabbit skeletal muscle protein phosphatases C-I and C-II / Steven R. Silberman, Maria Speth, Ramakrishna Nemani, Mahrukh K. Ganapathi, Viktor Dombrádi, Herve Paris, Ernest Y. C. Lee
Dátum:	1984
ISSN:	1083-351X
Megjegyzések:	Previous studies have shown that phosphorylase phosphatase can be isolated from rabbit liver and bovine heart as a form of Mr approximately 35,000 after an ethanol treatment of tissue extracts. This enzyme form was designated as protein phosphatase C. In the present study, reproducible methods for the isolation of two forms of protein phosphatase C from rabbit skeletal muscle to apparent homogeneity are described. Protein phosphatase C-I was obtained in yields of up to 20%, with specific activities toward phosphorylase a of 8,000-16,000 units/mg of protein. This enzyme represents the major phosphorylase phosphatase activity present in the ethanol-treated muscle extracts. The second enzyme, protein phosphatase C-II, had a much lower specific activity toward phosphorylase a (250-900 units/mg). Phosphatase C-I and phosphatase C-II had Mr = 32,000 and 33,500, respectively, as determined by sodium dodecyl sulfate disc gel electrophoresis. The two enzymes displayed distinct enzymatic properties. Phosphatase C-II was associated with a more active alkaline phosphatase activity toward p-nitrophenyl phosphate than was phosphatase C-I. Phosphatase C-II activities were activated by Mn2+, whereas phosphatase C-I was inhibited. Phosphatase C-I was inhibited by rabbit skeletal muscle inhibitor 2 while phosphatase C-II was not inhibited. Both enzymes dephosphorylated glycogen synthase and phosphorylase kinase, but displayed different specificities toward the alpha- and beta-subunit phosphates of phosphorylase kinase (Ganapathi, M. K., Silberman, S. R., Paris, H., and Lee, E. Y. C. (1980) J. Biol. Chem. 246, 3213-3217). The amino acid compositions of the two proteins were similar. Peptide mapping of the two proteins showed that they are distinct proteins and do not have a precursor-proteolytic product relationship.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban protein phosphatase C-I protein phosphatase C-II külföldön készült közlemény
Megjelenés:	The Journal of Biological Chemistry. - 259 : 5 (1984), p. 2913-2922. -
További szerzők:	Speth, Maria Nemani, Ramakrishna Ganapathi, Mahrukh K. Paris, Herve Lee, Ernest Y. C. Dombrádi Viktor (1953-) (biokémikus)
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat
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