Isolation of cardiac myofibrils and myosin light chains with in vivo levels of light chain phosphorylation.
Biochim Biophys Acta
; 587(4): 628-37, 1979 Nov 01.
Article
em En
| MEDLINE
| ID: mdl-228754
ABSTRACT
Conditions are described for the preparation of functional myofibrils and myosin light chains from freeze-clamped beating hearts with the state of light chain phosphorylation chemically 'frozen' during the extraction procedure. Myofibrils were shown to be functionally intact by measurement of Ca2+ binding and ATPase activity. Highly purified cardiac myosin light chains could be routinely isolated from myofibrillar preparations using ethanol fractionation together with ion-exchange chromatography. Analysis of light chains for covalent phosphate indicated that basal levels of phosphorylation of the 18--20 000 dalton light chain of myosin in rabbit hearts beating in situ or in a perfusion apparatus were 0.3--0.4 mol/mol. Covalent phosphate content of the light chain fraction did not change during perfusion of hearts with 10 microM epinephrine.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Miosinas
/
Miocárdio
/
Miofibrilas
Limite:
Animals
Idioma:
En
Ano de publicação:
1979
Tipo de documento:
Article