Exchange of 20-kDa myosin light chain-bound phosphate during sustained contraction of arterial smooth muscle.

Abstract:

:K(+)-contracted porcine carotid arterial muscles containing phosphorylated 20-kDa myosin light chains (LC) were exposed to carrier-free [32P]orthophosphate in K(+)-stimulating solution during sustained contraction. The covalently bound LC phosphate was completely replaced by [32P]phosphate, indicating that myosin light chain phosphatase and kinase have ready access to the bound phosphate during the sustained contraction. On average, 0.38 mol [32P]phosphate was incorporated per mole LC during the sustained K+ contraction. This value was about half of the maximal value for [32P]phosphate incorporation into LC, 0.74 mol/mol, in muscles contracted with K+ for 1 min. Assuming that sustained contraction involves the maximal number of cross-bridges attached to actin, the data suggest that half of the attached cross-bridges contain phosphorylated LC.

journal_name

Arch Biochem Biophys

authors

Bárány M,Rokolya A,Bárány K

doi

10.1016/0003-9861(91)90407-a

subject

Has Abstract

pub_date

1991-05-15 00:00:00

pages

199-203

issue

1

eissn

0003-9861

issn

1096-0384

pii

0003-9861(91)90407-A

journal_volume

287

pub_type

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