Arginine Specific Aminopeptidase from Lactobacillus brevis
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چکیده
منابع مشابه
Purification and characterization of an arginine aminopeptidase from Lactobacillus sakei.
An arginine aminopeptidase (EC 3.4.11.6) that exclusively hydrolyzes basic amino acids from the amino (N) termini of peptide substrates has been purified from Lactobacillus sakei. The purification procedure consisted of ammonium sulfate fractionation and three chromatographic steps, which included hydrophobic interaction, gel filtration, and anion-exchange chromatography. This procedure resulte...
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The pyruvate metabolism of LactobaciUus plantarum and Latobacillus arabino8su, which according to Bergey (1948) are identical organisms, has been studied by Rowatt (1951) and Nossal (1952). Both these homofermentative lactobacilli were shown to form 3-hydroxybutan-2-one (acetoin) as the main product of their pyruvate metabolism. No one appears to have studied the metabolism of pyruvate by any o...
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متن کاملGlutamate decarboxylase from Lactobacillus brevis: activation by ammonium sulfate.
In this study, the glutamate decarboxylase (GAD) gene from Lactobacillus brevis IFO12005 (Biosci. Biotechnol. Biochem., 61, 1168-1171 (1997)), was cloned and expressed. The deduced amino acid sequence showed 99.6% and 53.1% identity with GAD of L. brevis ATCC367 and L. lactis respectively. The His-tagged recombinant GAD showed an optimum pH of 4.5-5.0, and 54 kDa on SDS-PAGE. The GAD activity a...
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ژورنال
عنوان ژورنال: Brazilian Archives of Biology and Technology
سال: 2011
ISSN: 1516-8913
DOI: 10.1590/s1516-89132011000100018