l -Asparaginase from Proteus vulgaris

Abstract

To produce an immunologically and enzymologically new type of l -asparaginase, 108 strains of bacteria were screened for enzyme production. As a result, 13 bacteria belonging to the genera Alcaligenes, Bacterium , and Proteus were found to produce l -asparaginases in high levels. Among these l -asparaginases, partially purified l -asparaginases from B. cadaveris and P. vulgaris showed antitumor activity. A partially purified l -asparaginase preparation of P. vulgaris did not react with the antibody of Escherichia coli l -asparaginase on the Ouchterlony agar plate. Culture conditions for the production of l -asparaginase by P. vulgaris were investigated in detail. The enzyme was produced in high yields when cells were grown aerobically in a medium containing sodium fumarate and corn steep liquor. The addition of glucose or ammonium ion to the medium, however, resulted in depressed production of l -asparaginase. Under the optimum conditions, 3,700 international units of l -asparaginase was obtained from 1 liter of culture medium.

L-Asparaginase form Proteus vulgaris. Purification, crystallization, and enzymic properties

“…From the results above mentioned, P. vulgaris L-asparaginase seems to have a character quite similar to that of the E. coli enzyme. The two enzymes differ, however, with respect to immunochemical properties (Tosa et al, 1971). Some physicochemical properties and subunit structure of the P. vulgaris L-asparaginase will be reported elsewhere.…”

“…Enzyme Reactions. Unless otherwise noted, L-asparaginase activity was determined under the standard conditions previously described (Tosa et al, 1971). For the studies on hydrolytic rate of D-asparagine, L-glutamine, D-glutamine, Y-amethyl-L-asparagine, Y-a-carbobenzoxy-L-asparagine, laspartic acid /3-hydrazide, S-carbamyl-L-cysteine, 2-amino-2carboxyethanesulfonamide, n-butyramide, propionamide, and amino acid hydroxamates, the enzyme reaction was carried out under standard conditions substituting these compounds for L-asparagine.…”

Industrial effluent as a substrate for glutaminase freel-asparaginase production from Pseudomonas plecoglossicida strain RS1; media optimization, enzyme purification and its characterization

“…L-Asparaginase (EC 3.5.1.1) has been used as therapeutic remedy for acute lymphoblastic leukemia (ALL) wherein lymphoblasts are auxotrophic for L-asparagine, and the enzyme diminishes the supply of exogenous asparagine, thus forcing the tumor cells into apoptosis. 1,2 The antineoplastic activity of Lasparaginase has been explored from microbial sources such as Escherichia coli, 3,4 Proteus vulgaris, 5 Serratia marcescens, 6,7 Bacillus sp., 8 Pseudomonas aeruginosa, 9 Streptomyces sp., 10,11 Aspergillus terreus, 12 and Erwinia carotovora. 13 The substrate specicity of L-asparaginase is characterized for both L-asparagine and L-glutamine where L-glutamine differs from L-asparagine by a single methyl group, consequently Lasparaginase treatment diminishes L-glutamine availability along with the concentration of L-asparagine, causing side effects like leucopenia, acute pancreatitis, hyperglycemia and neurological seizures in ALL patients.…”

L-Asparaginase from Proteus vulgaris. Subunit and amino acid composition

“…In spite of similarities in some physicochemical properties for L-asparaginases from P. vulgaris and E. coli, the immunochemical properties of the two enzymes are different (Tosa et al,, 1971). Phillips et al, (1971) reported L-asparaginase from Serratia marcescens cross-reacted with anti-£.…”

“…On the other hand, we found that L-asparaginase from Proteus vulgaris has an antitumor activity and differs immunochemically from the E. coli enzyme (Tosa et al, 1971). We isolated the enzyme in a crystalline form and studied some enzymic properties of the crystalline enzyme (Tosa Methods Enzyme Assay.…”