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Glial Metabolism of Isoleucine [PDF]

open access: possibleNeurochemical Research, 2008
Isoleucine, together with leucine and valine, constitutes the group of branched-chain amino acids (BCAAs). BCAAs are transported from the blood into the brain parenchyma, where they can serve several distinct functions. Since brain tissue is known to oxidatively metabolize BCAAs to CO(2), they are considered as fuel material in brain energy metabolism.
Radovan Murín   +3 more
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Inhibition of Escherichia coli isoleucine biosynthesis by isoleucine tetrazole

Journal of Bacteriology, 1975
Growth of a derivative of Escherichia coli K-10 was strongly inhibited by 2 times 10(-4) M L-5(1-amino-2-methylbutyl)-tetrazole (isoleucine tetrazole). Growth inhibition was reversed by isoleucine, threonine, glycyl-L-isoleucine, or glycyl-L-threonine, and, in a valine-resistant mutant, by L-valine.
H Tristram, G A Willshaw
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Isoleucine production in bifidobacteria [PDF]

open access: possibleEuropean Journal Of Applied Microbiology, 1976
About 300 strains of bifidobacteria were examined for their capacity to release L-isoleucine in the fermentation broth. A strain of the speciesBifidobacterium ruminale was selected as the best producer. After treatment of this strain with NTG a DL-α-aminobutyric acid-resistant mutant capable of producing about 5 mg/ml of L-isoleucine in presence of 1.5
Diego Matteuzzi   +4 more
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Isoleucine and Allo-isoleucine

Nature, 1958
DURING our investigations on amino-acid analysis on ion exchange resins using Moore and Stein's method1, it was seen that in a synthetic mixture of 13 amino-acids (Hoffmann-LaRoche, mostly in the l-configuration) the ‘methionine’ recovery was always too high (120–150 per cent of the theoretical amount) and the ‘isoleucine’ recovery always too low (65 ...
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Biological availability of isoleucine

Archives of Biochemistry and Biophysics, 1957
Abstract Biological availability of isoleucine in eight different proteins was determined using a blood meal diet low in isoleucine. Isoleucine in zein was available to the extent of 30%; in casein and gelatin, around 60–70%; and in fibrin, beef, egg albumin, and Drackett, over 90% of the isoleucine was available to the rat.
A. E. Harper   +3 more
openaire   +3 more sources

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