Studies on the soluble phosphodiesterases of chicken gizzard smooth muscle.
Biochem J
; 215(3): 627-36, 1983 Dec 01.
Article
en En
| MEDLINE
| ID: mdl-6318728
In this study we describe the identification of four soluble forms of cyclic nucleotide phosphodiesterase from chicken gizzard smooth muscle. These isoenzymes were separated from one another by ion-exchange chromatography on DEAE-cellulose and by calmodulin-Sepharose affinity chromatography. Each form migrates as a single discrete band when it is electrophoresed on non-denaturing polyacrylamide gels and stained for phosphodiesterase activity. Each form is also eluted as a single peak on gel-permeation chromatography, giving apparent Mr values of 114 000, 116 000, 122 000 and 59 000. All four enzymes have apparent Km values in the 0-20 microM range, although their relative specificities for cyclic AMP and cyclic GMP differ. Two of the forms bind to calmodulin in a Ca2+-dependent manner; however, only one is activated by calmodulin. The interaction of the second calmodulin-binding form with calmodulin is disrupted by the papaverine derivative verapamil without significantly altering the hydrolytic activity of the enzyme.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
3',5'-AMP Cíclico Fosfodiesterasas
/
3',5'-GMP Cíclico Fosfodiesterasas
/
Isoenzimas
/
Músculo Liso
Tipo de estudio:
Prognostic_studies
Límite:
Animals
Idioma:
En
Revista:
Biochem J
Año:
1983
Tipo del documento:
Article
Pais de publicación:
Reino Unido