Two forms of NADP-dependent malic enzyme in expanding maize leaves

Planta ◽  
1979 ◽  
Vol 144 (3) ◽  
pp. 283-289 ◽  
Author(s):  
Paolo Pupillo ◽  
Patrizia Bossi
Keyword(s):  
Malic Enzyme ◽  
Maize Leaves

Interaction of divalent metal ions with the NADP+-malic enzyme from maize leaves

1991 ◽  
Vol 81 (4) ◽  
pp. 462-466 ◽  
Author(s):  
Maria Fabiana Drincovich ◽  
Alberto A. Iglesias ◽  
Carlos S. Andreo
Keyword(s):  
Metal Ions ◽  
Malic Enzyme ◽  
Divalent Metal ◽  
Divalent Metal Ions ◽  
Maize Leaves

Kinetic mechanism of NADP-malic enzyme from maize leaves

1995 ◽  
Vol 43 (1) ◽  
pp. 1-9 ◽  
Author(s):  
Claudia P. Spampinato ◽  
Carlos S. Andreo
Keyword(s):  
Malic Enzyme ◽  
Kinetic Mechanism ◽  
Maize Leaves

scholarly journals Evidence for the Existence of Two Essential and Proximal Cysteinyl Residues in NADP-Malic Enzyme from Maize Leaves

1992 ◽  
Vol 100 (4) ◽  
pp. 2035-2040 ◽  
Author(s):  
María F. Drincovich ◽  
Claudia P. Spampinato ◽  
Carlos S. Andreo
Keyword(s):  
Malic Enzyme ◽  
Maize Leaves

Two forms of NAD-malic enzyme in maize leaves are regulated by light in opposite ways via promoter methylation

2020 ◽  
Vol 251 ◽  
pp. 153193
Author(s):  
Alexander T. Eprintsev ◽  
Dmitry N. Fedorin ◽  
Marina O. Gataullina ◽  
Abir U. Igamberdiev
Keyword(s):  
Promoter Methylation ◽  
Malic Enzyme ◽  
Maize Leaves

A study on the inactivation of maize leaves nadp-malic enzyme by 3-bromopyruvate

1992 ◽  
Vol 31 (6) ◽  
pp. 1883-1888 ◽  
Author(s):  
Maria F. Drincovich ◽  
Carlos S. Andreo
Keyword(s):  
Malic Enzyme ◽  
Maize Leaves

scholarly journals NADP-linked malic enzyme. Purification from maize leaves, Mr and subunit composition

1988 ◽  
Vol 254 (1) ◽  
pp. 229-233 ◽  
Author(s):  
M S Thorniley ◽  
K Dalziel
Keyword(s):  
Malic Enzyme ◽  
Enzyme Purification ◽  
Gel Filtration ◽  
Sedimentation Velocity ◽  
Exchange Chromatography ◽  
Subunit Composition ◽  
Sedimentation Equilibrium ◽  
Apparent Homogeneity ◽  
Maize Leaves ◽  
A Subunit

1. The isolation of NADP-linked malic enzyme (EC 1.1.1.40) from maize leaves is described, together with studies of its Mr and subunit composition. 2. The enzyme was purified to apparent homogeneity by affinity chromatography on N6-aminohexyl-2′,5′-bisphosphoadenosine-agarose, gel filtration with Sephadex G-100 and ion-exchange chromatography on DEAE-Sephadex A-50. A purification of 140-fold with a 30% yield was obtained. 3. A detailed study of the Mr by several methods revealed the existence of different Mr forms in solution. 4. In the presence of dithiothreitol the enzyme appears to be present in triethanolamine buffer, pH 7.5, as a tetramer with a subunit Mr of 60,000 and an S20,w of 10.75 S. 5. In phosphate buffer, pH 7.0, it seems to be a dimer of Mr 120,000 with an S20,w of 7.95 S. 6. In the absence of dithiothreitol, lower-Mr forms were detected by sedimentation-equilibrium and sedimentation-velocity studies in triethanolamine buffer. 7. Results from gel filtration gave Mr values of about 340,000 in both buffers.

Interaction of divalent metal ions with the NADP+-malic enzyme from maize leaves

1991 ◽  
Vol 81 (4) ◽  
pp. 462-466 ◽  
Author(s):  
Maria Fabiana Drincovich ◽  
Alberto A. Iglesias ◽  
Carlos S. Andreo
Keyword(s):  
Metal Ions ◽  
Malic Enzyme ◽  
Divalent Metal ◽  
Divalent Metal Ions ◽  
Maize Leaves

Presence of Vicinal Dithiols in the NADP-Malic Enzyme from Maize Leaves

1992 ◽  
pp. 855-858
Author(s):  
Carlos S. Andreo ◽  
Claudia P. Spampinato ◽  
Maria F. Drincovich
Keyword(s):  
Malic Enzyme ◽  
Maize Leaves ◽  
Vicinal Dithiols
Sign in / Sign up

Export Citation Format

Share Document