Asparaginase and Glutaminase Activities of Micro-organisms
نویسندگان
چکیده
منابع مشابه
Human pharmacology and toxicology of succinylated Acinetobacter glutaminase-asparaginase.
AGA3 also had a very short half-life in humans (8). Chemical modification of free amino groups can increase the plasma half-life of some asparaginase and glutaminase-aspa raginase enzymes in animals (12, 20). In previous studies, we have shown that treatment of AGA with succinic anhydnide produces a uniform preparation with the same catalytic activity and physical properties, but with an increa...
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Concern about the rising prevalence of antibiotics-resistant strains of pathogenic microorganisms has been expressed in the last three decades. However, intensive studies on extracts and biologically-active compounds isolated from medicinal plants have also doubled in the last decade. As a result of paucity of knowledge and folkloric claim on the leaves effectiveness in infectious diseas...
متن کاملPhysical properties of Acinetobacter glutaminase-asparaginase with antitumor activity.
Acinetobaclet glutaminase-asparaginase has been shown to consist of 4 subunits (molecular weight 33,000) by sedimentation equilibrium in 5.5 M guanidine HCl and electrophoresis in sodium dodecyl sulfate on polyacrylamide gels after cross-linking the protein with dimethyl suberimidate. Moving boundary velocity experiments showed that most of the native enzyme sediments as the tetramer (SZO+ = 7....
متن کاملPhase I evaluation of succinylated Acinetobacter glutaminase-asparaginase in adults.
Succinylated Acinetobacter glutaminase-asparaginase (SAGA) has broader antitumor activity than Escherichia coli L-asparaginase in experimental systems; moreover, drug resistance does not develop in tumor cell lines initially sensitive to this enzyme. We have investigated the pharmacology and toxicology of SAGA after both single-dose and serial daily dose injections in 20 adult patients. Glutami...
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Glutaminase-asparaginase from Pseudomonas 7A appears to have four subunits with a molecular weight of 36,000 +/- 500 by sedimentation equilibrium in 5.9 M guanidine HCl and 34,000 by amino acid analysis. Analytic sedimentation equilibrium of the native enzyme showed a molecular weight of 140,000 +/- 3,300 with no signs of association or dissociation. Moving boundary and zone sedimentation in bu...
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ژورنال
عنوان ژورنال: Journal of General Microbiology
سال: 1973
ISSN: 0022-1287
DOI: 10.1099/00221287-76-1-85