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Titolo:
UNPHOSPHORYLATED ALPHA-PKC EXHIBITS PHORBOL ESTER BINDING BUT LACKS PROTEIN-KINASE ACTIVITY INVITRO
Autore:
FILIPUZZI I; FABBRO D; IMBER R;
Indirizzi:
UNIV HOSP BASEL,FRAUENSPITAL,DEPT GYNECOL & OBSTET,SCHANZENSTR 46 CH-4031 BASEL SWITZERLAND UNIV HOSP BASEL,FRAUENSPITAL,DEPT GYNECOL & OBSTET,SCHANZENSTR 46 CH-4031 BASEL SWITZERLAND CIBA GEIGY AG,DIV PHARMACEUT RES CH-4002 BASEL SWITZERLAND
Titolo Testata:
Journal of cellular biochemistry
fascicolo: 1, volume: 52, anno: 1993,
pagine: 78 - 83
SICI:
0730-2312(1993)52:1<78:UAEPEB>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
BREAST CANCER-CELLS; DOWN-REGULATION; C-GAMMA; RECEPTOR; PURIFICATION; EXPRESSION; DOMAINS; BRAIN;
Keywords:
PROTEIN EXPRESSION IN ESCHERICHIA-COLI; ENZYME ACTIVATION; POSTTRANSLATIONAL PHOSPHORYLATION; ALPHA-PKC;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
25
Recensione:
Indirizzi per estratti:
Citazione:
I. Filipuzzi et al., "UNPHOSPHORYLATED ALPHA-PKC EXHIBITS PHORBOL ESTER BINDING BUT LACKS PROTEIN-KINASE ACTIVITY INVITRO", Journal of cellular biochemistry, 52(1), 1993, pp. 78-83

Abstract

Expression of the alpha-isoform of protein kinase C (alpha-PKC) in E.coli yielded the unphosphorylated 74 kD precursor molecule. This precursor form exhibited phospholipid- and calcium-dependent phorbol esterbinding but lacked, in contrast to the phosphorylated enzyme, proteinkinase activity. In addition, the precursor molecule was found to interact with both threonine and an ATP analogon, which demonstrates thatphosphorylation of alpha-PKC is not required for binding of substrates, cofactors, or activators. These results, therefore, suggest that posttranslational phosphorylation of alpha-PKC is not needed for the formation of a functional enzyme-substrate complex but is necessary for the catalytic transfer of phosphate residues from ATP to protein substrates.

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Documento generato il 09/04/20 alle ore 06:47:48