Wheat Invertases | Zendy

Hari B. Krishnan | Zendy; Joan T. Blanchette | Zendy; Thomas W. Okita | Zendy

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Wheat Invertases

Author(s) -

Hari B. Krishnan,

Joan T. Blanchette,

Thomas W. Okita

Publication year - 1985

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.78.2.241

Subject(s) - invertase , concanavalin a , coleoptile , chromatography , polyacrylamide gel electrophoresis , biochemistry , chemistry , polyacrylamide , enzyme , cellulose , cell wall , protein subunit , sepharose , electrophoresis , hydrolysis , polymer chemistry , in vitro , gene

Wheat coleoptiles have two distinct invertases, a soluble and a cell wall-bound form as indicated by results from cytochemical and biochemical studies. These enzyme activities differ in their pH optima, chromatographic behavior on diethylaminoethyl cellulose, kinetic properties, thermal stability, and response to light treatment. The soluble invertase was purified to near homogeneity by diethylaminoethyl-cellulose, concanavalin-A Sepharose, and Sephacryl S-300 chromatography. The overall purification was 175-fold with a recovery of about 26%. The holoenzyme has an apparent molecular weight of 158,000 and subunit molecular weight of 53,000 as estimated by polyacrylamide gel electrophoresis under denaturing conditions. Illumination of wheat seedlings caused an increase in the cell wall, but not the soluble, invertase activity.

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