Literature DB >> 19400047

Hexosediphosphatase from spinach chloroplasts: purification, crystallization and some properties.

A M El-Badry1.   

Abstract

Hexosediphosphatase (D-fructose-1,6-bisphosphate 1-phosphohydrolase, EC 3.1.3.11) has been isolated, purified, and crystallized, from previously isolated spinach chloroplasts. The effects of various anions, cations, and sulfhydryl compounds were tested, and activation by Mg2+, glycine, HCO3-, and sulfhydryl compounds is described. The purified enzyme is very specific for fructose 1,6-diphosphate and does not attack sedoheptulose-1,7-bisphosphate. The S20 value of the enzyme was 7.7, from which the molecular weight of the enzyme was estimated as 140,000.

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Year:  1974        PMID: 19400047     DOI: 10.1016/0005-2728(74)90019-x

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  1 in total

1.  A new procedure for the purification of spinach leaf photosynthetic fructose-1,6-bisphosphatase by affinity chromatography on mercaptoethylamine-Sepharose.

Authors:  A Plá; A Chueca; J López-Gorgé
Journal:  Photosynth Res       Date:  1981-12       Impact factor: 3.573

  1 in total

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