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l isoleucine/karijes
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Crystal structure of the novel amino-acid racemase isoleucine 2-epimerase from Lactobacillus buchneri.
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Crystal structures of Lactobacillus buchneri isoleucine 2-epimerase, a novel branched-chain amino-acid racemase, were determined for the enzyme in the apo form, in complex with pyridoxal 5'-phosphate (PLP), in complex with N-(5'-phosphopyridoxyl)-L-isoleucine (PLP-L-Ile) and in complex with
Changes in activity levels and isozyme patterns of isoleucine aminotransferase in response to experimentally induced hepatic lesion.
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Branched-chain amino acid aminotransferase activities were measured in rats in which hepatic lesions were induced experimentally, that is, fatty liver produced by an orotic acid-containing diet and acute hepatic lesion induced by D-galactosamine injection into the abdominal cavity. The levels of the
Probing inclusion complexes of cyclodextrins with amino acids by physicochemical approach.
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Formations of host-guest inclusion complexes of two natural amino acids, viz., l-Leucine and l-Isoleucine as guests with α and β-cyclodextrins have been investigated which include diverse applications in modern science such as controlled delivery in the field of pharmaceuticals, food processing etc.
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