NDLI: Chloroplast thylakoid protein phosphatase is a membrane surface-associated activity.

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Chloroplast thylakoid protein phosphatase is a membrane surface-associated activity.

Content Provider	Semantic Scholar
Author	Sun, Guakin Bailey, Donald B. Jones, Michael Williamson Jana Kesavan Daryl
Copyright Year	1989
Abstract	Chloroplast thylakoid protein phosphatase activity was measured using (32)P-labeled histone as an exogenous substrate and an assay of the (32)Pi released involving formation of a phosphomolybdate complex and organic extraction. The activity was liberated from wheat (Triticum aestivum) thylakoids by washing the membranes in NaCl-containing solutions followed by centrifugation. The liberated phosphatase activity had a pH optimum of approximately 6.75, was inhibited by addition of 10 millimolar EDTA or EGTA, and was stimulated by addition of millimolar amounts of dithiothreitol, magnesium, manganese, or calcium ions. The rate of thylakoid protein dephosphorylation was decreased following liberation of a portion of the protein phosphatase activity and was increased by addition of salt-liberated phosphatase fraction. These results suggest that at least a portion of wheat thylakoid protein phosphatase is a peripheral, rather than an integral, membrane protein.
File Format	PDF HTM / HTML
Alternate Webpage(s)	https://digitalcommons.unl.edu/cgi/viewcontent.cgi?article=1326&context=biochemfacpub
PubMed reference number	16666520v1
Volume Number	89
Issue Number	1
Journal	Plant physiology
Language	English
Access Restriction	Open
Subject Keyword	Calcium ion Centrifugation Chloroplast thylakoids Chloroplasts Dithiothreitol Edetic Acid Egtazic Acid Histones Ions Magnesium Membrane Proteins Millimole per Liter Protein dephosphorylation Sodium Chloride Solutions Tissue membrane Tracer Triticum Wash (cleansing action) chloroplast proton-transporting ATP synthase complex phosphomolybdic acid phosphoric monoester hydrolase activity protein phosphatase activity thylakoid (cell component)
Content Type	Text
Resource Type	Article

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