STUDIES ON BIOSYNTHESIS OF CYCLITOLS .36. PURIFICATION OF MYO-INOSITOL-1-PHOSPHATE SYNTHASE OF DUCKWEED, LEMNA-GIBBA, TO HOMOGENEITY BY AFFINITY CHROMATOGRAPHY ON NAD-SEPHAROSE MOLECULAR AND CATALYTIC PROPERTIES OF ENZYME
- 1 January 1978
- journal article
- research article
- Vol. 359 (5) , 613-616
Abstract
Using the technique of affinity chromatography on NAD-Sepharose the myo-inositol-1-phosphate synthase of L. gibba was purified to homogeneity. The molecular and catalytic properties of this enzyme differ very much from those of myo-inositol-1-phosphate synthase from animal sources. Thus the specific activity of the duckweed enzyme is more than 2 orders of magnitude higher than that of the enzyme from rat testes. It is inhibited by EDTA and can be reactivated by Mn2. Its MW (135,000 .+-. 5000), its subunit composition (3 subunits with identical electrophoretic behavior) and its isoelectric point (pH 7.7) are also very different from the corresponding parameters for the animal enzyme.This publication has 5 references indexed in Scilit:
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