Characterization of Protein Phosphatase 2A Acting on Phosphorylated Plasma Membrane Aquaporin of Tulip Petals | Zendy

Abul Kalam Azad | Zendy; Yoshihiro Sawa | Zendy; Takahiro Ishikawa | Zendy; Hitoshi Shibata | Zendy

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Characterization of Protein Phosphatase 2A Acting on Phosphorylated Plasma Membrane Aquaporin of Tulip Petals

Author(s) -

Abul Kalam Azad,

Yoshihiro Sawa,

Takahiro Ishikawa,

Hitoshi Shibata

Publication year - 2004

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.68.1170

Subject(s) - dephosphorylation , phosphorylation , protein phosphatase 2 , petal , aquaporin , phosphatase , protein subunit , enzyme , biochemistry , membrane , acid phosphatase , substrate (aquarium) , microbiology and biotechnology , chemistry , biology , gene , botany , ecology

A protein phosphatase holo-type enzyme (38, 65, and 75 kDa) preparation and a free catalytic subunit (38 kDa) purified from tulip petals were characterized as protein phosphatase 2A (PP2A) by immunological and biochemical approaches. The plasma membrane containing the putative plasma membrane aquaporin (PM-AQP) was prepared from tulip petals, phosphorylated in vitro, and used as the substrate for both of the purified PP2A preparations. Although both preparations dephosphorylated the phosphorylated PM-AQP at 20 degrees C, only the holo-type enzyme preparation acted at 5 degrees C on the phosphorylated PM-AQP with higher substrate specificity, suggesting that regulatory subunits are required for low temperature-dependent dephosphorylation of PM-AQP in tulip petals.

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