scholarly journals Appropriate Thiamin Pyrophosphate Levels Are Required for Acclimation to Changes in Photoperiod

2019 ◽  
Vol 180 (1) ◽  
pp. 185-197 ◽  
Author(s):  
Laise Rosado-Souza ◽  
Sebastian Proost ◽  
Michael Moulin ◽  
Susan Bergmann ◽  
Samuel E. Bocobza ◽  
...  
1971 ◽  
Vol 121 (3) ◽  
pp. 431-437 ◽  
Author(s):  
Milton J. Allison ◽  
J. L. Peel

1. Growing cultures of Peptostreptococcus elsdenii and Bacteroides ruminicola incorporate 14C from [1-14C]isobutyrate into the valine of cell protein. With P. elsdenii some of the 14C is also incorporated into leucine. 2. Crude cell-free extracts of both organisms in the presence of glutamine, carbon dioxide and suitable sources of energy and electrons incorporate 14C from [1-14C]isobutyrate into valine but not into leucine. 3. With extracts of P. elsdenii treated with DEAE-cellulose the reaction is dependent on ATP, CoA, thiamin pyrophosphate, molecular hydrogen and a low-potential electron carrier (ferredoxin, flavodoxin or benzyl viologen). 4. The same extracts incorporate 14C from NaH14CO3 into valine in the presence of isobutyrate plus ATP, CoA, glutamine and ferredoxin; isobutyryl-CoA or isobutyryl phosphate plus CoA will replace the isobutyrate plus CoA and ATP. With acetyl phosphate in place of isobutyryl phosphate, 14C is incorporated into alanine. With isovalerate or 2-methylbutyrate in place of isobutyrate, 14C is incorporated into leucine and isoleucine respectively. 5. When carrier 2-oxoisovalerate is added to the carboxylating system 14C from [1-14C]isobutyrate passes into the oxo acid fraction. 6. It is concluded that these two organisms form valine from isobutyrate by the sequence isobutyrate→isobutyryl-CoA→2-oxoisovalerate→valine and that the reductive carboxylation of isobutyrate is catalysed by a system similar to the pyruvate synthetase of clostridia and photosynthetic bacteria.


1981 ◽  
Vol 34 (6) ◽  
pp. 1031-1033 ◽  
Author(s):  
D S McLaren ◽  
M A Docherty ◽  
D H Boyd

1983 ◽  
Vol 29 (12) ◽  
pp. 2073-2075 ◽  
Author(s):  
M Kimura ◽  
Y Itokawa

Abstract We demonstrate a liquid-chromatographic method involving post-column derivatization for determining the concentration of thiamin and its phosphate esters in human blood. Blood, erythrocytes, or plasma is deproteinized and centrifuged. Aliquots of the samples are applied to a mu Bondapak C18 column attached to a "high-performance" liquid chromatograph. Addition of potassium ferricyanide/sodium hydroxide solution to the column effluent with a proportioning pump converts thiamin phosphates into fluorophores, the intensities of which are measured with a spectrofluorophotometer. Thiamin, thiamin monophosphate, thiamin pyrophosphate, and thiamin triphosphate eluted as single peaks; no coeluting substances were detected. Thiamin pyrophosphate was the ester present in greatest concentration, followed by thiamin triphosphate; thiamin monophosphate and thiamin were present in slight amounts. This method allows easy determination of thiamin and its phosphate esters in 0.1 mL of blood.


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