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Title:
Isolation and properties of Ca2+-transporting glycoprotein and peptide from beef heart mitochondria | Journal of Bioenergetics and Biomembranes
Description:
The 40,000-dalton glycoprotein and 2000-dalton peptide inducing selective Ca2+-transport through bilayer lipid membranes were isolated from beef heart homogenate and mitochondria. Micromolar concentrations of these substances were found to increase the conductivity of membranes by 3β4 orders. Transmembrane Ca2+ gradient induces an electric potential difference whose magnitude is close to the theoretical for ideal Ca2+ selectivity. The inhibitor of mitochondrial Ca2+ transport, ruthenium red, abolishes both the glycoprotein-and peptide-induced Ca2+ transport in bilayer lipid membranes. Thiol groups essential for Ca2+ transport activity were revealed in the glycoprotein and peptide. Addition of these substances to rat liver mitochondria induces Ca2+-dependent inhibition of the state 3 respiration that can be released by uncouplers (oligomycin-like effect).
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Keywords {π}
google, scholar, mitochondria, transport, article, glycoprotein, mironova, membranes, pronevich, kondrashova, isolation, lipid, membrane, content, peptide, beef, heart, sirota, mironov, mitochondrial, biophys, chem, ussr, privacy, cookies, journal, catransporting, isolated, rat, liver, res, commun, biochem, publish, research, search, properties, trofimenko, access, mitochondriabiochem, systems, biol, data, information, log, bilayer, substances, induces, permeability, discover,
Topics {βοΈ}
low-molecular-weight ca2+ carrier insoluble ca2+-binding factor peptide-induced ca2+ transport soluble ca2+-binding glycoprotein month download article/chapter phospholipid thin-layer chromatography bilayer lipid membranes mitochondrial membrane permeability membrane-active substances isolated ca2+-transporting glycoprotein electric potential difference calcium-dependent processes human serum proteins mitochondrial ca2+ transport ca2+ transport activity ca2+ transport system induce selective transport ca2+-dependent regulation calcium transport membrane-active regulators privacy choices/manage cookies molecular weight determination rat liver mitochondria bimolecular lipid membranes ideal ca2+ selectivity ca2+-induced oscillations artificial lipid membranes related subjects low-toxicity solvent full article pdf ox liver mitochondria mitochondrial membrane soluble heat-labile beef heart mitochondria fully active papaine functionally active part european economic area frog cardiac muscle dried papaya latex elsevier/north-holland der papier chromatographie protein measurement folin phenol reagent sh group level influencing oxidative phosphorylation reversed electron transfer thiobarbituric acid assay conditions privacy policy sh-group content thiol groups essential
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headline:Isolation and properties of Ca2+-transporting glycoprotein and peptide from beef heart mitochondria
description:The 40,000-dalton glycoprotein and 2000-dalton peptide inducing selective Ca2+-transport through bilayer lipid membranes were isolated from beef heart homogenate and mitochondria. Micromolar concentrations of these substances were found to increase the conductivity of membranes by 3β4 orders. Transmembrane Ca2+ gradient induces an electric potential difference whose magnitude is close to the theoretical for ideal Ca2+ selectivity. The inhibitor of mitochondrial Ca2+ transport, ruthenium red, abolishes both the glycoprotein-and peptide-induced Ca2+ transport in bilayer lipid membranes. Thiol groups essential for Ca2+ transport activity were revealed in the glycoprotein and peptide. Addition of these substances to rat liver mitochondria induces Ca2+-dependent inhibition of the state 3 respiration that can be released by uncouplers (oligomycin-like effect).
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Organic Chemistry
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description:The 40,000-dalton glycoprotein and 2000-dalton peptide inducing selective Ca2+-transport through bilayer lipid membranes were isolated from beef heart homogenate and mitochondria. Micromolar concentrations of these substances were found to increase the conductivity of membranes by 3β4 orders. Transmembrane Ca2+ gradient induces an electric potential difference whose magnitude is close to the theoretical for ideal Ca2+ selectivity. The inhibitor of mitochondrial Ca2+ transport, ruthenium red, abolishes both the glycoprotein-and peptide-induced Ca2+ transport in bilayer lipid membranes. Thiol groups essential for Ca2+ transport activity were revealed in the glycoprotein and peptide. Addition of these substances to rat liver mitochondria induces Ca2+-dependent inhibition of the state 3 respiration that can be released by uncouplers (oligomycin-like effect).
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