Prenyl lipid formation in spinach chloroplasts and in a cell-free system of Synechococcus (Cyanobacteria): polyprenols, chlorophylls, and fatty acid prenyl esters

Planta ◽  
1985 ◽  
Vol 163 (1) ◽  
pp. 68-74 ◽  
Author(s):  
F. L�tke-Brinkhaus ◽  
G. Weiss ◽  
H. Kleinig
Keyword(s):  
Fatty Acid ◽  
Free System ◽  
Cell Free System ◽  
Spinach Chloroplasts ◽  
Lipid Formation ◽  
A Cell

Wirkung von Antikörpern gegen die Ferredoxin-NADP-Reduktase aus Spinat auf photosynthetische Reaktionen in einem zellfreien System aus der Blaualge Anacystis nidulans / Effect of Antibodies against Ferredoxin-NADP-Reductase from Spinach on Photosynthetic Reactions in a Cell-free System of Anacystis nidulans

1970 ◽  
Vol 25 (5) ◽  
pp. 529-534 ◽  
Author(s):  
Hermann Bothe ◽  
Richard J. Berzborn
Keyword(s):  
Anacystis Nidulans ◽  
Free System ◽  
Cell Free System ◽  
Spinach Chloroplasts ◽  
Cyclic Photophosphorylation ◽  
A Cell ◽  
Photosynthetic Reactions

Particles from Anacystis nidulans were obtained which - similar to preparations from spinachwere deficient in ferredoxin or in both ferredoxin and ferredoxin-NADP-reductase. The photosynthetic NADPH2-formation in these particles could be restored by addition of both these factors. The ferredoxin-NADP-reductase isolated from Anacystis closely ressembled in its enzymatical behaviour that enzyme from spinach. As previously described antibodies prepared against the spinach ferredoxin-NADP-reductase always inhibited the activities of the enzyme in spinach chloroplasts, regardless of whether the enzyme is bound to particles or made soluble. Contrary to this, in Anacystis these antibodies only affected the activities of the solubilized, but not of the particle-bound enzyme. Hence the reductase must be at least as tightly bound in the photosynthetic structure of Anacystis as it is in chloroplasts. The antibodies did not affect the ferredoxin-catalysed cyclic photophosphorylation in spinach and in Anacystis; this indicates that at least in spinach the ferredoxin-NADP-reductase is not involved in cyclic photophosphorylation.

scholarly journals Cell-free acylation of rat brain myelin proteolipid protein and DM-20

1987 ◽  
Vol 246 (3) ◽  
pp. 611-617 ◽  
Author(s):  
T Yoshimura ◽  
D Agrawal ◽  
H C Agrawal
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Palmitic Acid ◽  
Rat Brain ◽  
Polyacrylamide Gel Electrophoresis ◽  
Proteolipid Protein ◽  
Free System ◽  
Cell Free System ◽  
Selective Labelling ◽  
A Cell

Incubation of rat brain myelin with [3H]palmitic acid in the presence of ATP, CoA and MgCl2 or [14C]-palmitoyl-CoA in a cell-free system resulted in the selective labelling of ‘PLP’ [proteolipid protein; Folch & Lees (1951) J. Biol. Chem. 191, 807-817] and ‘DM-20’ [Agrawal, Burton, Fishman, Mitchell & Prensky (1972) J. Neurochem. 19, 2083-2089] which, after polyacrylamide-gel electrophoresis in SDS, were revealed by fluorography. These results provide evidence of the association of fatty acid-CoA ligase and acyltransferase in isolated myelin. Palmitic acid is covalently bound to PLP and DM-20, because 70 and 92% of the radioactivity was removed from proteolipid proteins after treatment with hydroxylamine and methanolic NaOH respectively. Incubation of myelin with [3H]palmitic acid in the absence of ATP, CoA, MgCl2, or all three, decreased incorporation of fatty acid into PLP to 3, 55, 18 and 2% respectively. The cell-free system exhibits specificity with respect to the chain length of the fatty acids, since myristic acid is incorporated into PLP at a lower rate when compared with palmitic and oleic acids. The acylation of PLP is an enzymic reaction, since (1) maximum incorporation of [3H]palmitic acid into PLP occurred at physiological temperatures and decreased with an increase in the temperature; (2) acylation of PLP with [3H]palmitic acid and [14C]palmitoyl-CoA was severely inhibited by SDS (0.05%); and (3) the incorporation of fatty acid and palmitoyl-CoA into PLP was substantially decreased by the process of freezing-thawing and freeze-drying of myelin. We have provided evidence that all of the enzymes required for acylation of PLP and DM-20 are present in isolated rat brain myelin. Acylation of PLP in a cell-free system with fatty acids and palmitoyl-CoA suggests that a presynthesized pool of non-acylated PLP and DM-20 is available for acylation.

scholarly journals Effect of detergents on sterol synthesis in a cell-free system of yeast

1982 ◽  
Vol 23 (6) ◽  
pp. 803-810
Author(s):  
S Hata ◽  
T Nishino ◽  
N Ariga ◽  
H Katsuki
Keyword(s):  
Sterol Synthesis ◽  
Free System ◽  
Cell Free System ◽  
A Cell

scholarly journals Reconstitution of Endosomal Proteolysis in a Cell-free System

1989 ◽  
Vol 264 (10) ◽  
pp. 5392-5399
Author(s):  
L S Mayorga ◽  
R Diaz ◽  
P D Stahl
Keyword(s):  
Free System ◽  
Cell Free System ◽  
A Cell
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