Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.5.1.1 (asparaginase)
 2,695 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. L-asparaginase from M. phlei was purified about 170-fold with an 11% yield. The purification procedure consisted of: fractionation with ammonium sulphate; adsorption of contaminating proteins on calcium phosphate gel; chromatography on Sephadex G-150 and DEAE-cellulose. The specific activity of the final preparation was 32.6 i.u./mg protein. 2. Molecular weight of the enzyme as determined by Sephadex G-100 filtration amounted to 126 000. Optimum pH was 8.8-9.2. The enzyme did not hydrolyse L-glutamine over the pH range 4-9, and was inhibited by D-asparagine. The apparent Michaelis constant for L-asparagine was 0.7 mM; energy of activation, 9800 cal/mole. 3. On polyacrylamide-gel electrophoresis the final preparation revealed two protein bands, one of which was coincident with the enzyme activity.
Acta Biochim Pol 1976
PMID:Purification and properties of L-asparaginase from Mycobacterium phlei. 0 91

1. L-Asparaginase has been isolated from aerobically grown Escherichia coli 055:B5 and purified about 140-fold in a three-step procedure involving acidification to pH 4.5, ammonium sulphate fractionation and column chromatography on DEAE-Sephadex A-50. The activity of the preparation is 140 U/mg protein. 2. The enzyme acts within a broad pH range (pH 5-9) and is affected neither by PCMB, N-ethylmaleimide nor metal ions. 3. Molecular weight of the isolated asparaginase is 130 000.
Acta Biochim Pol 1977
PMID:Purification and properties of L-asparaginase EC-2 from Escherichia coli 055:B5. 1 56

Seven Mycobacterium strains were grown statically on salts-glycerol-asparagine (Sauton) or on salts-glucose-glutamate (Sym) media. At desired time of incubation, the bacteria were washed with water, disintegrated with powdered corundum and in resulting cell-free extracts L-asparaginase activity was determined by the Conway method. The majority of experiments were performed on M. phlei which exhibited considerable rise in L-asparaginase activity with increasing age of the culture. This change did not occur on Sym medium because of Zn2+, which proved to abolish the effect of the enzyme induction in vivo but did not inhibit the activity in vitro. Addition of rifampicin to Sauton culture media resulted in a low enzyme level. Exogenous asparagine and glycerol were not indispensable for the enzyme synthesis and could be replaced by glutamate and glucose, respectively.
Acta Microbiol Pol A 1975
PMID:L-asparaginase activity of Mycobacterium phlei under various growth conditions. 24 89

The authors analysed 58 consecutive cases of acute leukaemia treated during 3.5 years. The material included 35 patients with myeloblastic leukaemia, 2 with pyomyelocytic leukaemia, 3 with monocytic leukaemia, 2 with erythroleukaemia, 7 with lymphoblastic leukaemia, and 8 with myeloblastic exacerbations of chronic myelocytic leukaemia. Most patients were treated by the VAMP schedule, in some cases L asparaginase, in other rubidomycin and cytosine arabinoside were used for obtaining remissions. Fourteen patients died within 14 days after admission to hospital. In 15 cases partial remissions, rather short-lasting, were achieved. In 4 cases the remissions were complete and in 3 of them the survival exceeds now 3 years. All patients in whom long-lasting remissions were obtained belonged to the youngest age group and 3 had lymphoblastic leukaemia. The authors suggest the need of rapid institution of treatment and systematic continuation.
Acta Haematol Pol
PMID:[Results of treatment of acute luekemia in adults according to our records]. 105 3

The regulation mechanism of production of staphylococcal L-asparaginase was investigated. The role of cAMP in regulation of its synthesis was confirmed. Production of L-asparaginase from S. aureus NCTC 4135 was inhibited by all carbon sources, mono- and disaccharides added to the growth medium. The strongest inhibition was caused by saccharose and maltose, whereas weaker by galactose, lactose, mannitol and mannose. It was found that exogenous cAMP in the presence of carbon sources stimulated synthesis of the investigated enzyme.
Acta Microbiol Pol 1992
PMID:Staphylococcal L-asparaginase: catabolic repression of synthesis. 128 44

A case of a 11-year girl with the acute lymphoblastic leukemia is presented. Patient was treated with L-asparaginase and developed a transient but lasting several weeks diabetes mellitus with ketoacidosis as a sequelae of this therapy.
Pol Tyg Lek
PMID:[Transient diabetes mellitus with ketoacidosis in a child during the treatment of acute lymphoblastic leukemia with L-asparaginase]. 140 32

Staphylococcal L-asparaginase inhibits blastic transformation of human lymphocytes and growth of mice leukemia lymphoblasts L5178Y-R. The enzyme is removed from blood stream of DBA/2 mice very rapidly.
Acta Microbiol Pol 1991
PMID:Staphylococcal L-asparaginase: antilymphoma and immunosuppressive action. 172 14

The ph optimum of purified staphylococcal L-asparaginase (EC 3.5.1.1) was found to be between 8.6 and 8.8. The temperature optimum was 30 degrees-32 degrees C and the highest reaction rate occurred at 30 degrees C. The KM of the enzyme calculated from Lineweaver-Burk plot was 3.71 x 10(-2) M. Besides L-asparaginase, the substrate specificity of enzyme was restricted to N-alpha-acetyl-L-asparagine. D-asparagine, L-aspartic acid and D-glutamic acid were competitive inhibitors. Hg2+ and Cu2+ cations strongly inhibited the enzyme while Na+ and K+ cations strongly stimulated activity. Two SH-groups could be detected after enzyme denaturation with guanidine.
Acta Microbiol Pol 1991
PMID:Staphylococcal L-asparaginase: enzyme kinetics. 172 15

Staphylococcal L-asparaginase has been purified 400-fold with 40% recovery. The procedure involves ammonium sulphate precipitation and a column chromatography on Sephadex G-200 gel filtration). The enzyme is composed of not identical subunits. protein (pI 4.4) with the approximate molecular weight of 125,000 (estimated by Sephadex G-200 gel filtration). The enzyme is composed of not identical subunits. The polyacrylamide-SDS gel electrophoresis indicated two subunits with molecular weight 18,000 and 22,000.
Acta Microbiol Pol 1989
PMID:Staphylococcal L-asparaginase: purification and properties of enzymic protein. 248 41

An ascogenous yeast with high potentialities for L-glutaminase and L-asparaginase formation was isolated from Egyptian soils by the application of the culture enrichment method. The organism, identified as Pichia polymorpha, was obtained through the enrichment of soil samples with a simple medium containing 0.5% L-glutaminase as a major carbon and nitrogen source at low pH values. The amidase activities were produced constitutively on a variety of media irrespective of the presence of their substrates in the growth medium. Assays of enzyme activity have revealed that optimum pH values for L-glutamine and L-asparagine hydrolysis are 6.0 and 6.7, respectively. The L-asparaginase activity of the cells was heat-stable for at least 10 minutes at 60 degrees C. The enzyme exhibited apparent Km of 1.37 x 10(-2) M and 1.95 x 10(-2) M for L-asparagine and L-glutamine, respectively. No metal requirement were detected for the amidase activities of the organism under study.
Acta Microbiol Pol 1980
PMID:Formation and properties of L-glutaminase and L-asparaginase activities in Pichia polymorpha. 616 54


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