Protein involvement in thermally induced structural transitions of pig erythrocyte ghosts

Autor:	Ahmik L. Jones, César Cobaleda, Enrique Villar, Fernando Leal, Galina G. Zhadan, Valery L. Shnyrov
Rok vydání:	1997
Předmět:	congenital hereditary and neonatal diseases and abnormalities Hot Temperature Swine Quantitative Biology::Tissues and Organs Physics::Medical Physics Clinical Biochemistry Analytical chemistry Biochemistry Quantitative Biology::Subcellular Processes Differential scanning calorimetry Erythrocyte Ghosts Genetics Animals Structural transition Molecular Biology Quantitative Biology::Biomolecules Calorimetry Differential Scanning Chemistry digestive oral and skin physiology Erythrocyte Membrane Sorption Cell Biology Blood Proteins Hydrogen-Ion Concentration Transport inhibitor Irreversible denaturation Covalent bond Biophysics Thermodynamics Electrophoresis Polyacrylamide Gel
Zdroj:	Europe PubMed Central
ISSN:	1039-9712
Popis:	Thermal transitions in pig erythrocyte ghosts were studied by differential scanning calorimetry and thermal gel analysis (TGA). Heating of the suspension of pig erythrocyte ghosts induced at least six thermodynamically irreversible transitions. Each of these transitions is believed to be due to a localized structural transition induced by thermal stress. Using TGA and covalent attachment of the anionic transport inhibitor regions in the thermograms corresponding to the heat sorption of some proteins of the pig erythrocyte ghosts were identified.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ab7acf21eeeeb108469d368ab97129a https://pubmed.ncbi.nlm.nih.gov/9192080 Zobrazit plný text záznamu Plný text