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Titolo:
EVIDENCE OF TRUE PROTEIN-KINASE CKII ACTIVITY IN MITOCHONDRIA AND ITSSPERMINE-MEDIATED TRANSLOCATION TO INNER MEMBRANE
Autore:
SARROUILHE D; BAUDRY M;
Indirizzi:
FAC MED PHARM,GRP RECH ETUD ANALOGUE MED,BP 199,34 RUE JARDIN PLANTESF-86005 POITIERS FRANCE
Titolo Testata:
Cellular and molecular biology
fascicolo: 2, volume: 42, anno: 1996,
pagine: 189 - 197
SICI:
0145-5680(1996)42:2<189:EOTPCA>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
RAT-LIVER MITOCHONDRIA; CASEIN KINASE; ENDOGENOUS PHOSPHORYLATION; CELLULAR-REGULATION;
Keywords:
PROTEIN PHOSPHORYLATION; PROTEIN KINASE CKII; MITOCHONDRIA; SPERMINE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
25
Recensione:
Indirizzi per estratti:
Citazione:
D. Sarrouilhe e M. Baudry, "EVIDENCE OF TRUE PROTEIN-KINASE CKII ACTIVITY IN MITOCHONDRIA AND ITSSPERMINE-MEDIATED TRANSLOCATION TO INNER MEMBRANE", Cellular and molecular biology, 42(2), 1996, pp. 189-197

Abstract

A true protein kinase CKII (CKII) activity was characterized in livermitochondria by its phosphorylating activity on the specific peptide substrate of CKII, the binding and elution profile of the enzyme on a phosphocellulose column and immunostaining of a 36 kDa polypeptide with antibodies against the cx-subunit of human CKII. This CKII activity was located predominantly in the intermembrane space of quiescent mitochondria. A translocation of the enzyme to inner membrane of energizedmitochondria occurred in the presence of spermine. Translocated CKII activity was tightly bound to inner membrane, and high salt concentrations were necessary to release the activity. The inner face of the inner membrane could constitute the in vivo localization of mitochondrialCW since the potential substrates of the enzyme are 4 matrix proteins.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/01/21 alle ore 11:29:15