High affinity interactions of Pb2+ with synaptotagmin I
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چکیده
منابع مشابه
Vesicle-associated membrane protein-2/synaptobrevin binding to synaptotagmin I promotes O-glycosylation of synaptotagmin I.
Synaptotagmin I (Syt I), an evolutionarily conserved integral membrane protein of synaptic vesicles, is now known to regulate Ca2+-dependent neurotransmitter release. Syt I protein should undergo several post-translational modifications before maturation and subsequent functioning on synaptic vesicles (e.g. N-glycosylation and fatty acylation in vertebrate Syt I), because the apparent molecular...
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Synaptotagmin I is a synaptic vesicle associated membrane protein that appears to regulate Ca(2+)-mediated exocytosis. Here, the Ca(2+)-dependent membrane interactions of a water soluble fragment of synaptotagmin I (C2AB) that contains its two C2 domains (C2A and C2B) were determined using site-directed spin labeling. Membrane depth parameters were obtained for 19 spin-labeled mutants of C2AB w...
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Columns containing immobilized lipoproteins were prepared for the analysis of drug interactions with these particles by high-performance affinity chromatography (HPAC). This approach was evaluated by using it to examine the binding of high-density lipoprotein (HDL) to the drugs propranolol and verapamil. HDL was immobilized by the Schiff base method onto silica and gave HPAC columns with reprod...
متن کاملInteractions of Apolipoprotein A-I with High-Density Lipoprotein Particles
Although the partitioning of apolipoprotein A-I (apoA-I) molecules in plasma between high-density lipoprotein (HDL)-bound and -unbound states is an integral part of HDL metabolism, the factors that control binding of apoA-I to HDL particles are poorly understood. To address this gap in knowledge, we investigated how the properties of the apoA-I tertiary structure domains and surface characteris...
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ژورنال
عنوان ژورنال: Metallomics
سال: 2018
ISSN: 1756-5901,1756-591X
DOI: 10.1039/c8mt00135a