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Purification, separation and characterization of phosphoglucomutase and phosphomannomutase from maize leaves
Author(s) -
Popova T. N.,
Matasova L. V.,
Lapotko A. A.
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549800203982
Subject(s) - phosphoglucomutase , phosphate , mannose , molecular mass , chemistry , enzyme , biochemistry , homogeneous , endosperm , isozyme , phosphofructokinase 2 , biology , chromatography , physics , thermodynamics
Different phosphomutases‐phosphogluconmtase (EC 2.7.5.1; PGM) and phosphomannomutase (EC 2.7.5.7; PMM) from maize (Zea mays L.) leaves have been purified. PGM and PMM were completely separated from each other. The purified PGM was shown to be electrophoretically homogeneous. The PGM fiom maize leaves was found to be a homodimer with an apparent molecular mass of 132 kDa, the size of the subunits was 66 kDa. The PGM is a bifunctional enzyme, which can use both glucose‐1‐ phosphate and mannose‐1‐phosphate as substrates. In contrast, the PMM appears to be monospecific for mannose‐1‐phosphate. Evidence is presented that PMM differs from PGM. Some properties of the maize leaves PGM and PMM differ in many respects (Km for substrates, pH optimum). However, some properties of PGM and PMM were similar (influence of Mg2+ and Mn2+ ions).