Physical properties of antitumor glutaminase-asparaginase from Pseudomonas 7A

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 +/-...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of biological chemistry 1976-09, Vol.251 (17), p.5375-5380
Main Authors: Holcenberg, J S, Teller, D C
Format: Article
Language:English
Subjects:
Amino Acids - analysis
Animals
Antineoplastic Agents
Asparaginase - therapeutic use
Biological Assay
Glutaminase - therapeutic use
Macromolecular Substances
Mathematics
Mice
Molecular Weight
Pseudomonas - enzymology
Species Specificity
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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 buffer showed normal behavior with sedimentation coefficients of 7.92 and 7.75 S, respectively. In contrast, the enzyme appeared to polymerize during zone sedimentation when the initial protein concentration was greater than 1 mg/ml and the buffer contained asparagine, glutamine, or 5-diazo-4-oxonorvaline. An extension of our method for active enzyme sedimentation is described which utilizes the changes in absorption during hydrolysis of asparagine by low concentrations of enzyme. Polymerization was not seen under these conditions.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(17)33171-X