Physiology of L-asparaginase synthesis in recombinants of Escherichia coli A-1
نویسندگان
چکیده
منابع مشابه
Production and optimization of L-asparaginase in Escherichia coli
-ASPARAGINASE (L-ASNase) has been widely used as a therapeutic agent in the treatment for various lymphoblastic leukemia diseases. This study aimed to isolate and purify local bacterial isolates that are capable of producing L-ASNase, so 150 bacterial isolates from the Nile River where isolated, purified and their ability to produce L-ASNase was assessed. Among these isolates, 32 bacterial isol...
متن کاملProduction of L-asparaginase II by Escherichia coli.
l-Asparaginase II was synthesized at constant rates by Escherichia coli under anaerobic conditions. The enzyme was produced optimally by bacteria grown between pH 7 and 8 at 37 C. Although some enzyme was formed aerobically, between 100 and 1,000 times more asparaginase II was produced during anaerobic growth in media enriched with high concentrations of a variety of amino acids. Bacteria grown...
متن کاملCrystal packing of plant-type L-asparaginase from Escherichia coli.
Plant-type L-asparaginases hydrolyze the side-chain amide bond of L-asparagine or its beta-peptides. They belong to the N-terminal nucleophile (Ntn) hydrolases and are synthesized as inactive precursor molecules. Activation occurs via the autoproteolytic release of two subunits, alpha and beta, the latter of which carries the nucleophile at its N-terminus. Crystallographic studies of plant-type...
متن کاملcomparison of catalytic activity of heteropoly compounds in the synthesis of bis(indolyl)alkanes.
heteropoly acids (hpa) and their salts have advantages as catalysts which make them both economically and environmentally attractive, strong br?nsted acidity, exhibiting fast reversible multi-electron redox transformations under rather mild conditions, very high solubility in polar solvents, fairly high thermal stability in the solid states, and efficient oxidizing ability, so that they are imp...
15 صفحه اولL-Asparaginase from escherichia coli B. Succinylation and subunit interactions.
Asparaginase from Esckerickio coli B has been modified with increasing amounts of [r4C]succinic anhydride. Enzyme activity is enhanced when 15 % and 25 % of the lysyl residues are succinylated. Up to 40% of the lysyl residues were succinylated without destroying enzyme activity and without causing dissociation of this oligomeric protein. More extensive succinylation causes dissociation into sub...
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ژورنال
عنوان ژورنال: Applied and Environmental Microbiology
سال: 1978
ISSN: 0099-2240,1098-5336
DOI: 10.1128/aem.35.4.766-770.1978