Results 261 to 270 of about 241,731 (297)
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Tightly-bound divalent cation of actin
Journal of Muscle Research and Cell Motility, 1992Actin is known to undergo reversible monomer-polymer transitions that coincide with various cell activities such as cell shape changes, locomotion, endocytosis and exocytosis. This dynamic state of actin filament self-assembly and disassembly is thought to be regulated by the properties of the monomeric actin molecule and in vivo by the influence of ...
J E, Estes +3 more
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Divalent cations induce protofibril gelation
American Journal of Hematology, 1988AbstractSoluble fibrin oligomers (protofibrils) undergo phase change merely by adding 1–2 mM Ca2+ 25‐100 μM Zn2+. The cation‐induced “protofibrin” clots appear similar to normally formed fibrin gels. Maximal clot turbidity of protofibrin gels increases with cations in a concentration‐dependent manner.
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O-Carboxymethylagar: interaction with divalent cations
Carbohydrate Polymers, 1994Abstract O -Carboxymethylagar was produced from a commercial, low methoxylated agar sample. The degree of substitution of the sample was 1·2 carboxymethyl groups per disaccharide repeating unit. The procedure used for the synthesis lowered the polymer molecular weight slightly.
Bosco M., GAMINI, AMELIA, RIZZO, ROBERTO
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Interaction of divalent cations, quinolones and bacteria
Journal of Antimicrobial Chemotherapy, 1994The interaction between divalent cations and quinolones and the mechanism by which the former antagonizes the antimicrobial activities of the latter were investigated. In the presence of either magnesium or calcium chloride, the MICs of 18 quinolones for Gram-positive and Gram-negative bacteria increased. Accumulation of and inhibition of DNA synthesis
A J, Marshall, L J, Piddock
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The effect of divalent cations on cell adhesion
Journal of Periodontal Research, 1969The effect of several divalent cations on cell adhesion was estimated in monolayer cell cultures. The exclusion of the divalent cations (Ca and Mg) from Hanks' balanced salt solution resulted in rapid cell detachment from the glass substratum. Detached cells would reattach when these divalent cations again were introduced into the medium.Other divalent
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An Overview of Divalent Cation and Citrate Handling by the Kidney
Nephron Physiology, 2004Urinary calcium, magnesium and citrate levels are important in promoting or inhibiting renal stone formation. Here we review current information on the tubular handling of these ions. Most filtered calcium is reabsorbed in the proximal tubule and the thick ascending limb (TAL) of the loop of Henle, largely paracellularly; most of the remainder is ...
Unwin R. +2 more
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The role of divalent cations in potassium channels
Trends in Neurosciences, 1988Abstract The most heterogeneous of the ion channel proteins may be those selective for potassium ions. This broad class of channels includes, among many others, voltage dependent potassium channels important for repolarizing nerve and muscle action potentials (so-called delayed rectifier K channels).
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Divalent cation dopants for polyparaphenylene
Synthetic Metals, 1993Abstract Free-standing films of polyparaphenylene (PPP) were synthesized from the electrochemical oxidation of benzene. A potential of about 4.7 V was applied across the counter and working electrodes in a nitrobenzene solution containing lithium hexafluoroarsenate and copper (II) chloride as electrolytes.
E.-W. Chang, R.J. Kuk, R.B. Kaner
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Divalent Cations, Nucleotides, and Actin Structure
2001Actin has one high-affinity site for a divalent cation, with a Kd for Ca2+ and Mg2+ in the nanomolar range. This binding site is located at the bottom of the cleft between the two domains of the molecule (Fig. 1). The cation is coordinated not only by amino acid residues but also by the oxygen of the γ- and/or β- phosphate groups of the nucleotide, ADP
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Potentiation of Acetylcholine Receptors by Divalent Cations
Molecular Pharmacology, 2006Divalent cations promote activation of several nicotinic acetylcholine receptor (AChR) subtypes, presumably by lowering the energetic barrier between open and closed conformations. In wild-type alpha7 AChRs, binding of calcium to a particular part of the extracellular domain is required for potentiating activation. McLaughlin et al. (p.
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