http://www.cnr.it/ontology/cnr/individuo/prodotto/ID259007

Halothane does not alter Ca2+ affinity of troponin C (Articolo in rivista)

Type

Prodotto della ricerca (Classe)
Articolo in rivista (Classe)

Label

Halothane does not alter Ca2+ affinity of troponin C (Articolo in rivista) (literal)

Anno

1992-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

10.1097/00000542-199201000-00015 (literal)

Alternative label

Blanck TJ, Chiancone E, Salviati G, Heitmiller ES, Verzili D, Luciani G, Colotti G. (1992)
Halothane does not alter Ca2+ affinity of troponin C
in Anesthesiology (Phila.); LIPPINCOTT-RAVEN PUBL, PHILADELPHIA (Stati Uniti d'America)
(literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

Blanck TJ, Chiancone E, Salviati G, Heitmiller ES, Verzili D, Luciani G, Colotti G. (literal)

Pagina inizio

100 (literal)

Pagina fine

105 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

76 (literal)

Rivista

Anesthesiology (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali

6 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

1 (literal)

Note

ISI Web of Science (WOS), Scopus (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

Department of Anesthesiology and Critical Care Medicine, Johns Hopkins University, Baltimore, Maryland. Dept. Biological Sciences University Sapienza. Centro Biologia Molecolare CNR (literal)

Titolo

Halothane does not alter Ca2+ affinity of troponin C (literal)

Abstract

Troponin C has been suggested as a possible target for the negative inotropic action of volatile anesthetics. This study has examined the effect of halothane on the structure and response of isolated cardiac troponin C to Ca2+ and the response of skinned soleus and cardiac muscle fibers to Ca2+. The high-affinity Ca(2+)-binding sites of cardiac troponin C were assessed by measurement of the change in intrinsic tyrosine fluorescence and ultraviolet circular dichroism in response to Ca2+ in the presence and absence of halothane. Halothane (0.9 mM, 1.4%) did not alter the 45% enhancement in intrinsic tyrosine fluorescence that occurs with saturation of the high-affinity sites or change the Ca2+ concentration at which half-maximal enhancement occurred. The molar ellipticity in the far ultraviolet region, a measure of the secondary structure, increased to a similar extent with addition of 10(-6) M Ca2+ in the absence and presence of 1.0 mM (1.6%) halothane. The binding rate of the sulfhydryl reagent, 5,5'-dithiobis (2-nitrobenzoic acid), to troponin C in response to Ca2+ titration was used as a measure of the integrity of the low-affinity Ca(2+)-binding site in troponin C in the presence and absence of 1.0 mM (1.6%) halothane. The rate of reaction was stimulated twofold, and the half maximal effect was observed at pCa 4.8 +/- 0.2 in both control and halothane-treated samples. Halothane (5 mM; 7.8%) did not change the pCa/tension response of skinned soleus fibers; the data were fit to the Hill equation and yielded dissociation constants of 6.2 x 10(-7) M for control and halothane-treated specimens. (literal)

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