Relative mobility and activity of leaf malate dehydrogenase in flax(Linum usitatissimum) genotrophs and genotypes

1988 ◽  
Vol 26 (3-4) ◽  
pp. 261-275 ◽  
Author(s):  
M. A. Fieldes
Keyword(s):  
Malate Dehydrogenase ◽  
Linum Usitatissimum ◽  
Relative Mobility

PROTEIN PROFILES OF FLAX GENOTROPHS

1982 ◽  
Vol 24 (4) ◽  
pp. 417-425 ◽  
Author(s):  
Mary Ann Fieldes ◽  
Hugh Tyson ◽  
David Marriott
Keyword(s):  
Linum Usitatissimum ◽  
Plant Proteins ◽  
Two Dimensional ◽  
Stem Tissue ◽  
Protein Profiles ◽  
Relative Mobility ◽  
Two Dimensional Electrophoresis ◽  
Linum Usitatissimum L ◽  
Flax Genotrophs ◽  
Dimensional Electrophoresis

Protein profiles of partially purified protein extracts from main stem tissue of Durrant's L and S flax (Linum usitatissimum L.) genotrophs were examined with one and two dimensional electrophoresis on acrylamide gels. The purification retained mainly glycoproteins. Among this reduced spectrum of plant proteins, some of the proteins separated had relative mobility (Rm) shifts between L and S. For two proteins, the Rm shifts were demonstrated in two-dimensional separations using mixtures of the L and S extracts. The Rm shifts were all in the same direction, the S protein ran slightly slower than the corresponding L protein, in both dimensions. This shift direction agreed with previous studies on Rm shifts with peroxidase and esterase isozymes and with similar shifts in acid phosphatase isozymes.

DIFFERENCES IN MOLECULAR WEIGHT BETWEEN CORRESPONDING ANIONIC PEROXIDASE ISOZYMES FROM TWO FLAX GENOTROPHS

1980 ◽  
Vol 22 (4) ◽  
pp. 529-534 ◽  
Author(s):  
H. Tyson ◽  
M. A. Fieldes
Keyword(s):  
Molecular Weight ◽  
Linear Regression ◽  
Linum Usitatissimum ◽  
Gel Electrophoresis ◽  
Relative Mobility ◽  
Anionic Peroxidase ◽  
Linum Usitatissimum L ◽  
Peroxidase Isozymes ◽  
Flax Genotrophs ◽  
Adult Plants

Anionic peroxidase isozymes from main stem tissues of adult plants of two flax (Linum usitatissimum L.) genotrophs were separated using acrylamide gel electrophoresis. A range of seven acrylamide concentrations was used for the gels, enabling the effect of gel concentration on relative mobility (Rm) to be examined. The regression of log (Rm) on gel concentration was linear for two of the four main isozymes found. Differences in linear regression slope between the L and S flax genotroph isozymes suggested genotroph differences in molecular weight.

ACTIVITY AND RELATIVE MOBILITY OF PEROXIDASE ISOENZYMES IN GENOTROPHS AND GENOTYPES OF FLAX (LINUM USITATISSIMUM L.)

1972 ◽  
Vol 14 (3) ◽  
pp. 625-636 ◽  
Author(s):  
M. A. Fieldes ◽  
H. Tyson
Keyword(s):  
Linum Usitatissimum ◽  
Gel Electrophoresis ◽  
Relative Mobility ◽  
Peroxidase Isoenzymes ◽  
Anionic Peroxidase ◽  
Linum Usitatissimum L ◽  
Phosphorus And Potassium ◽  
Highly Correlated ◽  
Successive Generations ◽  
Nitrogen Phosphorus

Acrylamide gel electrophoresis was used to separate anionic peroxidase isoenzymes in genotypes and genotrophs of flax. Activities and relative mobilities were measured directly from the separations on the gels.The effects of growth of one flax genotype in soil supplemented by either nitrogen, phosphorus and potassium (NPK) or nitrogen and potassium (NK) on subsequent generations of its progeny produced by complete selfing were studied. Both activity and relative mobility of anionic peroxidase isoenzymes displayed effects of fertilizer treatments applied in previous generations. NPK increased the relative mobility of all isoenzymes, while depressing the activity of at least three of them. Successive generations of growth in NPK produced approximately linear increases in relative mobility. Such environmentally induced heritable changes were detectable five generations later.Two other flax genotypes were crossed, and relative mobility and activity of anionic peroxidase isoenzymes were examined in both parents and F2 progeny. Between parents, there were differences in relative mobility for two of the four isoenzymes; their F2 hybrids showed intermediate mobility for these particular isoenzymes. There were no differences between reciprocal F2 hybrids for mobility or activity of any isoenzyme. The parents differed in activity in all four isoenzymes; the F2 hybrids displayed dominance towards the lower activity parent for each of the isoenzymes.Total anionic isoenzyme activity was highly correlated with gross peroxidase activity measured prior to electrophoretic separation.

ACTIVITY AND RELATIVE MOBILITY OF PEROXIDASE AND ESTERASE ISOZYMES OF FLAX (LINUM USITATISSIMUM) GENOTROPHS. I. DEVELOPING MAIN STEMS

1973 ◽  
Vol 15 (4) ◽  
pp. 731-744 ◽  
Author(s):  
M. A. Fieldes ◽  
H. Tyson
Keyword(s):  
Linum Usitatissimum ◽  
Relative Mobility ◽  
Esterase Isozymes ◽  
Anionic Peroxidase ◽  
Rates Of Change ◽  
Peroxidase Isozymes

The effects of growth of one flax genotype in soil supplemented by either nitrogen, phosphorous and potassium (NPK) or nitrogen and potassium (NK) on its progeny produced by several generations of complete selfing were studied. The two types of progeny produced, L induced by NPK and S induced by NK, were examined at 4-day intervals from the 16th to the 36th day after sowing. Both activity and relative mobility of the anionic peroxidase and esterase isozymes displayed effects of the fertilizer treatments applied in the treatment generation. NPK, compared to NK, increased the relative mobility of all the peroxidase and esterase isozymes, while depressing the activities of the peroxidase isozymes and increasing those of the esterase isozymes, at all ages examined. Some differences in the rates of change, with age, of the characteristics of L and S were distinguished; the differences observed between L and S could not, however, be attributed to differences in their developmental ages.

Light-activation of NADP-malate dehydrogenase: A highly controlled process for an optimized function

2000 ◽  
Vol 110 (3) ◽  
pp. 322-329 ◽  
Author(s):  
M. Miginiac-Maslow ◽  
K. Johansson ◽  
E. Ruelland ◽  
E. Issakidis-Bourguet ◽  
I. Schepens ◽  
...  
Keyword(s):  
Malate Dehydrogenase ◽  
Light Activation

SALT AND WATER BINDING TO HALOPHILIC MALATE DEHYDROGENASE

1984 ◽  
Vol 45 (C7) ◽  
pp. C7-269-C7-269
Author(s):  
G. Zaccai ◽  
E. Wachtel ◽  
H. Eisenberg
Keyword(s):  
Malate Dehydrogenase ◽  
Water Binding

Hepatoprotective activity and standardization of the bioactive lignan fraction of Linum usitatissimum L.

Planta Medica ◽  
2016 ◽  
Vol 81 (S 01) ◽  
pp. S1-S381
Author(s):  
H El-Askary ◽  
S El Zalabani ◽  
RS El-Din ◽  
MY Issa ◽  
RR Hegazy ◽  
...  
Keyword(s):  
Linum Usitatissimum ◽  
Hepatoprotective Activity ◽  
Linum Usitatissimum L
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