Published 1994
| Version v1
Journal article
Comparative studies of native and recombinant horseradish peroxidase upon irradiation and other inactivating factors
- 1. Moskovskij Gosudarstvennyj Univ., Moscow (Russian Federation)
Description
Comparative studies of native and recombinant horseradish peroxidase inactivation in the enzymatic reaction course under elevated temperatures and radiation have been performed. The protective effect of the carbohydrate component of the native peroxidase assuring the enzyme stabilization against different inactivating factors has been shown. It is suggested that radiation-induced inactivation leads to the changes in hemine interaction with the protein component and in the conformational mobility at the enzyme active center. 11 refs.; 5 figs
Additional details
Additional titles
- Original title (Russian)
- Сравнительное изучение стабильности нативной и рекомбинантной пероксидазы хрена под действием радиации и других инактивирующих факторов
Publishing Information
- Journal Title
- Izvestiya Akademii Nauk. Seriya Khimicheskaya
- Journal Issue
- no.12
- Journal Page Range
- p. 2230-2233.
- ISSN
- 0002-3353
- CODEN
- IASKEA
INIS
- Country of Publication
- Russian Federation
- Country of Input or Organization
- Russian Federation
- INIS RN
- 27055448
- Subject category
- S38: RADIATION CHEMISTRY, RADIOCHEMISTRY AND NUCLEAR CHEMISTRY;
- Descriptors DEI
- CHEMICAL RADIATION EFFECTS; CHEMICAL REACTION KINETICS; COMPARATIVE EVALUATIONS; DOSE RATES; GAMMA RADIATION; INACTIVATION; PEROXIDASES; RADIATION DOSES; STABILITY
- Descriptors DEC
- CARBOXYLIC ACIDS; ELECTROMAGNETIC RADIATION; ENZYMES; EVALUATION; HETEROCYCLIC ACIDS; HETEROCYCLIC COMPOUNDS; IONIZING RADIATIONS; KINETICS; ORGANIC ACIDS; ORGANIC COMPOUNDS; ORGANIC NITROGEN COMPOUNDS; OXIDOREDUCTASES; PORPHYRINS; PROTEINS; RADIATION EFFECTS; RADIATIONS; REACTION KINETICS