Comparative Studies on Soluble Lactonases
- 1 June 1962
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 51 (6) , 405-415
- https://doi.org/10.1093/oxfordjournals.jbchem.a127554
Abstract
Lactonase-I, aldonolactonase and gluconolaconase are concluded to be the same enzyme, as these enzymes showed the constant ratic of the activity on different substrates at various purification steps and they had the same properties, such as substrate specificity, metal requirement and species distribution. Sedimentation, electrophoresis and immunochemical analysis of purified lactonase- I were reported. Substrate specificity of' lactonase-I was described. Lactonase-I hydrolyzed gluconolactone, but did not act on 6-phosphogluconolactone. Presence of 6-phosphogluconolactonase (lacto nase-III) in mammalian tissue was evidenced. 6-Phosphogluconolactonase (lactonase-III) in mammalian tissue was concluded to be different from gluconolactonase reported by Brodie and Lipmann. The classification of lactonase was proposed.Keywords
This publication has 1 reference indexed in Scilit:
- Synthesis of D-glucose-1-C-14 and D-mannose-1-C-14Journal of Research of the National Bureau of Standards, 1952