Recent results on the active site of amine oxidases
- 1 May 1984
- journal article
- Published by Springer Nature in Inflammation Research
- Vol. 14 (3-4), 356-357
- https://doi.org/10.1007/bf01973826
Abstract
A preparation of bovine plasma amine oxidase, containing only one copper ion per molecule, was obtained by treatment with diethyldithiocarbamate. The enzyme preparation still retained full activity. Thus, only one of the two copper ions contained in the enzyme molecule appears to be involved in the catalytic process.Keywords
This publication has 9 references indexed in Scilit:
- Reaction of beef plasma and lentil seedlings Cu-amine oxidases with phenylhydrazineBiochemical and Biophysical Research Communications, 1983
- Purification of bovine plasma amine oxidaseAnalytical Biochemistry, 1982
- Properties of cupric ions in benzylamine oxidase from pig plasma as studied by magnetic-resonance and kinetic methodsBiochemical Journal, 1979
- Studies on the mechanism of action of plasma amine oxidaseBiochemistry, 1978
- Changes in the copper centres of benzylamine oxidase from pig plasma during the catalytic cycleBiochemical and Biophysical Research Communications, 1978
- Diamine Oxidase from Pig KidneyPublished by Elsevier ,1967
- DIAMINE OXIDASE FROM PIG KIDNEY - IMPROVED PURIFICATION AND PROPERTIES1967
- PURIFICATION OF AMINE OXIDASE FROM BEEF PLASMAJournal of Biological Chemistry, 1954
- A Micro Biuret Method for Protein Determination Determination of Total Protein in Cerebrospinal FluidScandinavian Journal of Clinical and Laboratory Investigation, 1953