Determination of polysaccharide linkage and branching by reductive depolymerization. Gas-liquid chromatography and gas-liquid chromatography-mass spectrometry reference data

1985 ◽  
Vol 143 ◽  
pp. 1-20 ◽  
Author(s):  
Agnes Van Langenhove ◽  
Vernon N. Reinhold
1988 ◽  
Vol 59 (1) ◽  
pp. 155-164 ◽  
Author(s):  
C. R. Krishnamurti ◽  
S. M. Janssens

1. Whole-body protein synthetic rates in non-pregnant ewes were determined by the continuous infusion of L-[15N]- and [1-13C]leucine and measuring the plasma enrichment of leucine, α-ketoisocaproate (α-KIC) and expired carbon dioxide by gas–liquid chromatography–mass spectrometry.2. The mean whole-body protein synthesis estimated from plasma leucine flux corrected for oxidation was 5·38 (SE 0·54) g/kg per d.3. Under the conditions of the present study leucine oxidation was 0·323 (SE 0·067) mmol/kg per d and accounted for 10·71 (SE 2·26) % of plasma [13C]leucine flux. Deamination of leucine was 0·55 (SE 0·035) mmol/kg per d and accounted for approximately 17% of plasma [15N]leucine flux.4. The rate of α-KIC reamination to leucine, calculated by subtracting 13C flux from 15N flux, was 0·228 (SE 0·101) mmol/kg per d.5. The rate of whole-body protein degradation was 4·49 (SE 0·54) g/kg per d and there was a net protein gain of 0·89 (SE 0·21) g/kg per d.


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