Published December 1994
| Version v1
Journal article
Comparative studies of stability of native and recombinant horseradish peroxidase inactivated by radiation and other factors
- 1. M.V. Lomonosov Moscow State Univ. (Russian Federation)
Description
Comparative studies of the inactivation of native and recombinant horseradish peroxidase in the course of an enzymatic reaction, at elevated temperatures and in a wide range of radiation doses, have been performed. The protective effect of the carbohydrate component of the native peroxidase providing for stabilization of the enzyme against various inactivating factors was demonstrated. It was proposed that radioactive inactivation is related to dysfunction in heme interaction with the protein component and to an increase in the conformational mobility around the active site of the enzyme
Additional details
Publishing Information
- Journal Title
- Russian Chemical Bulletin
- Journal Volume
- 43
- Journal Issue
- 12
- Journal Page Range
- p. 2110-2113.
- ISSN
- 1066-5285
- CODEN
- RCBUEY
INIS
- Country of Publication
- United States
- Country of Input or Organization
- United States
- INIS RN
- 27025502
- Subject category
- S63: RADIATION, THERMAL, AND OTHER ENVIRONMENTAL POLLUTANT EFFECTS ON LIVING ORGANISMS AND BIOLOGICAL MATERIALS;
- Resource subtype / Literary indicator
- Translation
- Descriptors DEI
- CHEMICAL RADIATION EFFECTS; ENZYME ACTIVITY; GENE RECOMBINATION; PEROXIDASES; RADIATION DOSES; STABILITY
- Descriptors DEC
- CARBOXYLIC ACIDS; ENZYMES; HETEROCYCLIC ACIDS; HETEROCYCLIC COMPOUNDS; ORGANIC ACIDS; ORGANIC COMPOUNDS; ORGANIC NITROGEN COMPOUNDS; OXIDOREDUCTASES; PORPHYRINS; PROTEINS; RADIATION EFFECTS
Optional Information
- Notes
- Translated from Izvestiya Akademii Nauk. Seriya Khimicheskaya; No. 12, 2230-2333(Dec 1994).