Preliminary crystal structure of Acinetobacter glutaminasificans glutaminase-asparaginase.
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چکیده
منابع مشابه
Physical 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...
متن کاملHuman 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...
متن کاملEffect of Acinetobacter glutaminase-asparaginase treatment on free amino acids in mouse tissues.
Acinetobacter glutaminase-asparaginase (AGA) and Escherichia coli asparaginase were compared for their effects on plasma and tissue levels of amino acids, ammonia, and glutamyl transferase activity in the mouse. Free asparagine was depleted similarly in plasma and tissues by both enzymes. AGA treatment produced partial depletion of glutamine concentrations in muscle, spleen, small intestine, an...
متن کاملEffect of Acinetobacter Glutaminase-Asparaginase Treatment on Free Amino Acids in Mouse Tissues1
Acinetobacier glutaminase-asparaginase (AGA) and Escherichia coli asparaginase were compared for their effects on plasma and tissue levels of amino acids, am monia, and glutamyl transferase activity in the mouse. Free asparagine was depleted similarly in plasma and tissues by both enzymes. AGA treatment produced partial depletion of glutamine concentrations in muscle, spleen, small intes tine, ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1988
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)57371-9