valine


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Related to valine: isoleucine, histidine, serine

valine

 [va´lēn]
a naturally occurring amino acid, one of the essential amino acids.
Miller-Keane Encyclopedia and Dictionary of Medicine, Nursing, and Allied Health, Seventh Edition. © 2003 by Saunders, an imprint of Elsevier, Inc. All rights reserved.

val·ine (Val, V),

(val'in),
2-Amino-3-methylbutanoic acid; the l-isomer is a constituent of most proteins; a nutritionally essential amino acid.
Farlex Partner Medical Dictionary © Farlex 2012

valine

(văl′ēn′, vā′lēn′)
n.
An essential amino acid, C5H11NO2.
The American Heritage® Medical Dictionary Copyright © 2007, 2004 by Houghton Mifflin Company. Published by Houghton Mifflin Company. All rights reserved.

val·ine

(V) (vā-lēn')
2-amino-3-methylbutanoic acid; the l-isomer is a constituent of most proteins; a nutritionally essential amino acid.
Medical Dictionary for the Health Professions and Nursing © Farlex 2012

valine

One of the ESSENTIAL AMINO ACIDS, a constituent of protein.
Collins Dictionary of Medicine © Robert M. Youngson 2004, 2005
Valineclick for a larger image
Fig. 313 Valine . Molecular structure.

valine (V, Val)

one of 20 AMINO ACIDS common in proteins. It has a nonpolar ‘R’ group structure and is relatively insoluble in water. See Fig. 313 . The ISOELECTRIC POINT of valine is 6.0.
Collins Dictionary of Biology, 3rd ed. © W. G. Hale, V. A. Saunders, J. P. Margham 2005

val·ine

(Val, V) (vā-lēn')
A nutritionally essential amino acid.
Medical Dictionary for the Dental Professions © Farlex 2012
References in periodicals archive ?
Valine and leucine, the branched-chain amino acids ([BCAA.sub.S]) participating in blood glucose regulation, were found to be signicantly increased in male and female rats within exhaustive exercise.
In above mentioned human studies, this position appeared non-synonymous similar to our samples, but in human studies it appeared as frame shift point mutation, while in our dogs' samples, it changed the valine residue to phenylalanine amino acid.
According to the need for biomarkers of AD specially in blood samples which has a less invasive method than collecting CSF fluid, also a serum metabolite marker panel was prpoposed for the detection of AD, including alanine, glutamine, serine, valine, isobutyrate, carnitine, taurine, pantothenate, glucose, asparagine, succinate, glycine, creatinine, isoleucine, pyruvate, betaine, choline, scyllo-inositol and myo-inositol.
LEU, leucine; ILEU, isoleucine; AILEU, allo-isoleucine; VAL, valine.
Peak Retention Amino acids Linear time (min) range ([micro]g/L) 1 8.87 Serine 8.45-101.46 2 10.98 Treonine 8.51-102.06 3 13.49 Arginine 8.36 100.28 4 14.26 Alanine 8.76-105.14 5 16.66 Proline 8.67-104.00 6 24.99 Valine 8.36-100.37 7 25.87 Methionine 8.35-100.19 8 26.95 Cysteine 8.27- 99.30 9 28.29 Isoleucine 8.29 -99.52 10 28.88 Tryptophan 8.30-99.54 Peak A b([10.
This study was conducted to determine the effects of altering the SID valine:lysine ratio on the performance and amino acid metabolism of 144 crossbred (Duroc x Landrace x Large White) pigs weaned at 28 [+ or -] 4 days of age and weighing 8.79 [+ or -] 0.02 kg body weight.
The increases for T2DM in leucine, isoleucine, valine, and 3-HIB were significant after BMI adjustment, but those in tyrosine and phenylalanine were not.
The amino acid profile revealed an isoleucine level of 5.9 [micro]mol/L, leucine of 1166 [micro]mol/L, and valine of 159 [micro]mol/L.
Following initial decompensation attack, medical supportive treatments were used during increases in blood leucine, valine, and isoleucine levels during infections for 19 months' follow-up period.
(4,12) Between 70% and 90% of BRAF mutations involve a single base transversion (T>A) in exon 15, which results in the substitution of glutamic acid for valine at amino acid position 600 (BRAF V600E) (Figure 3).
The effects of GanedenBC 30 with protein were examined in a random double blind crossover clinical trial on key amino acids including leucine (the regulator for muscle protein synthesis), isoleucine and valine (branched chain amino acids), as well as histidine, alanine, asparagines, citrulline, cystine, glutamine (a key amino acid for supporting ph balance and the immune system), methionine, ornthinine, serine, threonine, tryptophan and phenylalanine.
Usually, studies conducted to evaluate the reduction in crude protein by means of amino acid supplementation use only L-Lysine, DL-methionine, L-threonine and L-tryptophan, but, progressive CP reduction in diets may lead to a situation in which other amino acids, such as arginine, valine and isoleucine, act as limiting factors for improved performance (Peganova & Eder, 2002).