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PMID: 3027121 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Myosin specific phosphatases isolated from Dictyostelium discoideum.

Journal of muscle research and cell motility ·Vol. 7 ·No. 6 ·1986-12-00 ·Pages 510-6

Kuczmarski ER, Pagone J

Abstract

Using native myosin phosphorylated on either the heavy chain or the light chain, we have isolated myosin phosphatases from extracts of vegetative Dictyostelium amoeba. Two phosphatases were resolved by DEAE-cellulose chromatography. One of these phosphatases removed phosphate from heavy chain or light chain at approximately the same rate. The other phosphatase appeared to be much more specific for phosphorylated myosin heavy chain. Although these enzymes removed phosphate from other phosphoprotein substrates such as histone or casein, they did so at a much lower rate. Both enzymes required magnesium for activity, but appeared to be independent of calcium.

MeSH Terms
Animals Calcium/pharmacology Dictyostelium/enzymology Magnesium/pharmacology Myosin-Light-Chain Phosphatase Myosins/metabolism Phosphoprotein Phosphatases/isolation & purification Phosphorylation Substrate Specificity
Chemicals
Phosphoprotein Phosphatases Myosin-Light-Chain Phosphatase Myosins Magnesium Calcium
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Kuczmarski E R
Pagone J
References (25)
25 references, click to expand
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Article Info
Journal
Journal of muscle research and cell motility
Abbr.
J Muscle Res Cell Motil
ISSN
0142-4319
Published
1986-12-00
Pages
510-6
Language
English
Region
Netherlands
NLM ID
8006298
Subset
IM
Grants
NIGMS NIH HHS · GM 31907 · United States
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