Phosphorylation and actin activation of brain myosin.

B. Barylko, A. Sobieszek

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

A method is described for obtaining brain myosin that shows significant actin activation, after phosphorylation with chicken gizzard myosin light chain kinase. Myosin with this activity could be obtained only via the initial purification of brain actomyosin. The latter complex, isolated by a method similar to that used for smooth muscle, contained actin, myosin, tropomyosin of the non-muscle type and another actin-binding protein of approximately 100,000 daltons. From the presence of a specific myosin light chain kinase and phosphatase in brain tissue it is suggested that the regulation of actin-myosin interaction operates via phosphorylation and dephosphorylation of myosin.

Original languageEnglish (US)
Pages (from-to)369-374
Number of pages6
JournalEMBO Journal
Volume2
Issue number3
StatePublished - 1983

Fingerprint

Phosphorylation
Myosins
Actins
Brain
Chemical activation
Myosin-Light-Chain Kinase
Myosin-Light-Chain Phosphatase
Avian Gizzard
Microfilament Proteins
Actomyosin
Tropomyosin
Purification
Smooth Muscle
Muscle
Chickens
Tissue

ASJC Scopus subject areas

  • Genetics
  • Cell Biology

Cite this

Phosphorylation and actin activation of brain myosin. / Barylko, B.; Sobieszek, A.

In: EMBO Journal, Vol. 2, No. 3, 1983, p. 369-374.

Research output: Contribution to journalArticle

Barylko, B & Sobieszek, A 1983, 'Phosphorylation and actin activation of brain myosin.', EMBO Journal, vol. 2, no. 3, pp. 369-374.
Barylko, B. ; Sobieszek, A. / Phosphorylation and actin activation of brain myosin. In: EMBO Journal. 1983 ; Vol. 2, No. 3. pp. 369-374.
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