[Comparison of physico-chemical properties of two forms of dopamine-beta-hydroxylase from chromaffin granules]

Autor:	A S, Boiadzhan, R M, Nalbandian, G Kh, Buniatian
Rok vydání:	1981
Předmět:	Binding Sites Protein Conformation Osmolar Concentration Electron Spin Resonance Spectroscopy Dopamine beta-Hydroxylase Hydrogen-Ion Concentration Isoenzymes Kinetics Chromaffin System Animals Cattle Chromaffin Granules Copper Protein Binding
Zdroj:	Biokhimiia (Moscow, Russia). 46(4)
ISSN:	0320-9725
Popis:	The purification procedures of both soluble and membrane-bound forms of dopamine-beta-hydroxylase have been developed. The membrane-bound form was solubilized by a detergent. Both preparations have been obtained in electrophoretically homogeneous form. The yield of soluble and membrane-bound enzyme forms by a described procedure was 22 mg and 15 mg, correspondingly, from 100 g of chromaffin granules paste. A comparative analysis of the main physico-chemical properties of the two enzyme forms has shown their identity. The effects of pH, ionic strength, oxidants and reducers on the EPR spectra of the two forms of dopamine-beta-hydroxylase have been investigated. A comparison of the EPR spectra of the two forms of the enzyme suggests that the copper environment of soluble and membrane-bound dopamine-beta-hydroxylases is practically identical.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::7d3a2a70cf3b15a4de2335e6a728837e https://pubmed.ncbi.nlm.nih.gov/6269659 Zobrazit plný text záznamu