Acyl-CoA dehydrogenase activity in pea cotyledon tissue during germination and initial growth

2000 ◽  
Vol 28 (6) ◽  
pp. 760-762 ◽  
Author(s):  
C. Masterson ◽  
A. Blackburn ◽  
C. Wood
Keyword(s):  
Dehydrogenase Activity ◽  
Chain Length ◽  
Root Formation ◽  
Short Chain ◽  
Initial Growth ◽  
Chain Acyl ◽  
Pea Seeds ◽  
Acyl Coa Dehydrogenases ◽  
Hydroponically Grown ◽  
Long Chain

Acyl-CoA dehydrogenase activity has been measured in homogenates of post-imbibition to 14-day-old hydroponically grown pea seeds at daily intervals, using C4, C12 and C16 acyl-CoA substrates. The activity peaks of the different chain-length acyl-CoA dehydrogenases did not transpose at all points and the ratios of the chain-length activities were not constant. It therefore has to be concluded that more than one dehydrogenase is present in pea mitochondria. There was a post-imbibition initial surge of activity with short- and mid-chain-length substrates. The C16- handling enzyme first peaked at 3–4 days, which coincided with the onset of plumule unfurling and greening. Further peaks were observed with all three substrates, coinciding with secondary root formation and leaf enlargement and later with cotyledon degeneration. Overall activity showed that the long-chain acyl-CoA dehydrogenase was much more active than the short-chain acyl-CoA dehydrogenase.

scholarly journals Nonacosan-10-ol and n-Alkanes in Leaves of Pinus pinaster

2020 ◽  
Vol 15 (5) ◽  
pp. 1934578X2092607
Author(s):  
Biljana Nikolić ◽  
Marina Todosijević ◽  
Iris Đorđević ◽  
Jovana Stanković ◽  
Zorica S. Mitić ◽  
...  
Keyword(s):  
Chain Length ◽  
Pinus Pinaster ◽  
Cuticular Wax ◽  
Short Chain ◽  
Average Chain Length ◽  
Carbon Preference Index ◽  
Preference Index ◽  
Long Chain

In leaf cuticular wax of Pinus pinaster, content of nonacosan-10-ol is high (77.1% on average). n-Alkanes ranged from C18 to C35 with the most dominant C29 (24.8%). The carbon preference index (CPItotal) ranged from 3.1 to 5.6 (4.0 on average), while the average chain length (ACLtotal) ranged from 14.0 to 17.0 (14.8 on average). Long-chain n-alkanes ( n-C25-35) strongly dominated (80.1%) over middle-chain ( n-C21-24 = 18.9%) and short-chain ( n -C18-20 = 0.9%) n-alkanes.

scholarly journals A fixation procedure suitable for autoradiography of endogenous long-chain acyl carnitine.

1985 ◽  
Vol 33 (8) ◽  
pp. 744-748 ◽  
Author(s):  
M T Knabb ◽  
G G Ahumada ◽  
B E Sobel ◽  
J E Saffitz
Keyword(s):  
Subcellular Localization ◽  
Selective Extraction ◽  
Total Radioactivity ◽  
Water Soluble ◽  
Free Carnitine ◽  
Neonatal Rat ◽  
Short Chain ◽  
Tissue Processing ◽  
Chain Acyl ◽  
Long Chain

A tissue processing procedure was evaluated for fixation of endogenous long-chain acyl carnitine (LCA) to facilitate autoradiographic subcellular localization of this amphiphile. Suspensions of neonatal rat myocytes labeled with exogenous 14C-palmitoyl carnitine retained 85.2% of the radiolabel after tissue processing. Autoradiography demonstrated no significant translocation of radiolabeled LCA from myocytes to unlabeled sheep erythrocytes mixed in equal proportions and processed together. To evaluate endogenous LCA fixation, cultured myocytes were incubated for 3 days with 3H-carnitine. Radioactivity was distributed in LCA, short-chain acyl carnitine, and free carnitine pools in proportion to the physiological concentrations of the metabolites traced. Before tissue processing, LCA contained 4.5% of total radioactivity. After tissue processing, labeled water-soluble components were lost and 88% of the retained radioactivity was in the LCA pool. The enrichment of endogenous LCA radioactivity was attributable to the selective extraction of endogenous short-chain and free carnitine. Nearly 75% of endogenous LCA was preserved. In contrast, 99.5% of both endogenous short-chain and free carnitine were extracted. Thus, endogenous LCA can be selectively preserved, permitting quantitative subcellular localization of this amphiphile with ultrastructural autoradiography.

scholarly journals Acyl-CoA dehydrogenase activity in the riboflavin-deficient rat. Effects of starvation

1987 ◽  
Vol 244 (2) ◽  
pp. 387-391 ◽  
Author(s):  
N S Ross ◽  
C L Hoppel
Keyword(s):  
Fatty Acid ◽  
Dehydrogenase Activity ◽  
Fatty Acid Oxidation ◽  
Specific Activity ◽  
Short Chain ◽  
Acid Oxidation ◽  
Riboflavin Deficiency ◽  
Mitochondrial Fatty Acid ◽  
Chain Acyl ◽  
Riboflavin Deficient

Riboflavin deficiency in weanling rats causes a metabolic disorder characterized by failure to oxidize fatty acids. The disorder is similar to that seen in several human diseases, some of which are responsive to pharmacological doses of riboflavin. Previous analysis of the riboflavin-deficient rat has shown that the failure of fatty acid oxidation is due to a decrease in the activity of the acyl-CoA dehydrogenases of beta-oxidation. The activity of these flavoenzymes in liver rapidly decreases when a riboflavin-deficient diet is initiated. The objectives of these experiments were to analyse the effects of starvation on liver mitochondria isolated from the riboflavin-deficient rat. Our studies show that the decreased mitochondrial fatty acid oxidation induced by riboflavin deficiency is partially reversed by starvation. The extent of this reversal is proportional to the duration of starvation. The starvation-associated increase in fatty acid oxidation is mediated by an increase in the mitochondrial short-chain acyl-CoA dehydrogenase activity. The activity of this enzyme is increased such that the ratio of short-chain acyl-CoA dehydrogenase apoenzyme to holoenzyme does not change. We conclude that short-chain acyl-CoA dehydrogenase activity is limiting for fatty acid oxidation when its activity falls below a critical point. The increased mitochondrial specific activity of short-chain acyl-CoA dehydrogenase during starvation may result from an increased availability of flavin coenzyme or an increase in enzyme catalytic efficiency.

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