Seven days of oral taurine supplementation does not increase muscle taurine content or alter substrate metabolism during prolonged exercise in humans

2008 ◽  
Vol 105 (2) ◽  
pp. 643-651 ◽  
Author(s):  
Stuart D. R. Galloway ◽  
Jason L. Talanian ◽  
Anna K. Shoveller ◽  
George J. F. Heigenhauser ◽  
Lawrence L. Spriet

This study examined 1) the plasma taurine response to acute oral taurine supplementation (T), and 2) the effects of 7 days of T on muscle amino acid content and substrate metabolism during 2 h of cycling at ∼60% peak oxygen consumption (V̇o2peak). In the first part of the study, after an overnight fast, 7 volunteers (28 ± 3 yr, 184 ± 2 cm, 88.0 ± 6.6 kg) ingested 1.66 g oral taurine doses with breakfast (8 AM) and lunch (12 noon), and blood samples were taken throughout the day. In the second part of the study, eight men (22 ± 1 yr, 181 ± 1 cm, 80.9 ± 3.8 kg, 4.21 ± 0.16 l/min V̇o2peak) cycled for 2 h after 7 days of placebo (P) ingestion (6 g glucose/day) and again following 7 days of T (5 g/day). In the first part of the study, plasma taurine was 64 ± 4 μM before T and rose rapidly to 778 ± 139 μM by 10 AM and remained elevated at noon (359 ± 56 μM). Plasma taurine reached 973 ± 181 μM at 1 PM and was 161 ± 31 μM at 4 PM. In the second part of the study, seven days of T had no effect on muscle taurine content (mmol/kg dry muscle) at rest (P, 44 ± 15 vs. T, 42 ± 15) or after exercise (P, 43 ± 12 vs. T, 43 ± 11). There was no difference in muscle glycogen or other muscle metabolites between conditions, but there were notable interaction effects for muscle valine, isoleucine, leucine, cystine, glutamate, alanine, and arginine amino acid content following exercise after T. These data indicate that 1) acute T produces a 13-fold increase in plasma taurine concentration; 2) despite the ability to significantly elevate plasma taurine for extended periods throughout the day, 7 days of T does not alter skeletal muscle taurine content or carbohydrate and fat oxidation during exercise; and 3) T appears to have some impact on muscle amino acid response to exercise.

1965 ◽  
Vol 18 (2) ◽  
pp. 353 ◽  
Author(s):  
JH Bradbury ◽  
GV Chapman ◽  
NLR King

Ultrasonic disruption of powdered Merino wool in formic acid and dichloroacetic acid causes some protein to be dissolved, but the amino acid content of the residual wool is unchanged by the treatment. Cortical cells and disrupted cortical cells are found to have the same composition as the parent fibre, which is to be expected because the latter consists of about 90 % cortical cells. However, the cuticle of Merino wool is different in composition from the parent fibre, being richer in cysteic acid, serine, proline, glycine, valine, and cystine, and poorer in aspartic acid, threonine, glutamic acid, methionine, isoleucine, leucine, tyrosine, phenylalanine, and arginine than the whole fibre. Thus the cuticle is considerably less polar than the fibre as a whole. With the exceptions detailed below, it is found that the first group of amino acids listed above are classified as non a.helix.forming and the second group as a�helix� forming by Blout (1962). The exceptions are isoleucine and threonine, whilst arginine and glycine are not classified. It is therefore postulated that the cuticle is amorphous because of its high content of non a�helix.forming amino acids. The cuticle of Lincoln wool shows similar differences to those already given for Merino cuticle but, in addition, contains less lysine and histidine than the whole fibre.


1933 ◽  
Vol 27 (5) ◽  
pp. 1648-1654 ◽  
Author(s):  
James Murray Luck ◽  
Stanley Wallace Morse

2021 ◽  
Vol 19 (1) ◽  
pp. 35-43
Author(s):  
Awatsaya Chotekajorn ◽  
Takuyu Hashiguchi ◽  
Masatsugu Hashiguchi ◽  
Hidenori Tanaka ◽  
Ryo Akashi

AbstractWild soybean (Glycine soja) is a valuable genetic resource for soybean improvement. Seed composition profiles provide beneficial information for the effective conservation and utilization of wild soybeans. Therefore, this study aimed to assess the variation in free amino acid abundance in the seeds of wild soybean germplasm collected in Japan. The free amino acid content in the seeds from 316 accessions of wild soybean ranged from 0.965 to 5.987 mg/g seed dry weight (DW), representing a 6.2-fold difference. Three amino acids had the highest coefficient of variation (CV): asparagine (1.15), histidine (0.95) and glutamine (0.94). Arginine (0.775 mg/g DW) was the predominant amino acid in wild soybean seeds, whereas the least abundant seed amino acid was glutamine (0.008 mg/g DW). A correlation network revealed significant positive relationships among most amino acids. Wild soybean seeds from different regions of origin had significantly different levels of several amino acids. In addition, a significant correlation between latitude and longitude of the collection sites and the total free amino acid content of seeds was observed. Our study reports diverse phenotypic data on the free amino acid content in seeds of wild soybean resources collected from throughout Japan. This information will be useful in conservation programmes for Japanese wild soybean and for the selection of accessions with favourable characteristics in future legume crop improvement efforts.


2008 ◽  
Vol 43 (10) ◽  
pp. 1786-1791 ◽  
Author(s):  
Waldemar Kmiecik ◽  
Zofia Lisiewska ◽  
Jacek Słupski ◽  
Piotr Gębczyński

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