Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P50583 (asymmetrical)
 12,197 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The glutamine/amino acid transporter was solubilized from rat renal apical plasma membrane (brush-border membrane) with C12E8 and reconstituted into liposomes by removing the detergent from mixed micelles by hydrophobic chromatography on Amberlite XAD-4. The reconstitution was optimised with respect to the protein concentration, the detergent/phospholipid ratio and the number of passages through a single Amberlite column. The reconstituted glutamine/amino acid transporter catalysed a first-order antiport reaction stimulated by external, not internal, Na+. Optimal activity was found at pH 7.0. The sulfhydryl reagents HgCl2, mersalyl and p-hydroxymercuribenzoate and the amino acids alanine, serine, threonine, cysteine, asparagine, methionine and valine strongly inhibited the transport, whereas the amino acid analogue methylaminoisobutyrate had no effect. Glutamine, alanine, serine, asparagine, threonine were efficiently translocated from outside to inside and from inside to outside the proteoliposomes as well. Cysteine and valine were translocated preferentially from outside to inside. The Km for glutamine on the external and internal side of the transporter was 0.47 and 11 mM, respectively; the values were not influenced by the type of the counter substrate. The transporter is functionally asymmetrical and it is unidirectionally inserted into the proteoliposomal membrane with an orientation corresponding to that of the native membrane. By a bisubstrate kinetic analysis of the glutamine antiport, a random simultaneous mechanism was found. The glutamine antiport was strongly stimulated by internal nucleoside triphosphates and, to a lower extent, by pyrophoshate. The reconstituted glutamine/amino acid transporter functionally corresponds to the ASCT2 protein.
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PMID:Reconstitution into liposomes of the glutamine/amino acid transporter from renal cell plasma membrane: functional characterization, kinetics and activation by nucleotides. 1558 47

Reactions of Hg(OAc)2 with 2 equiv of TabHPF6 [TabH = 4-(trimethylammonio)benzenethiol] in MeCN/MeOH afforded a mononuclear linear complex [Hg(Tab)2](PF6)2 (1). By using 1 as a precursor, a new family of mercury(II) zwitterionic thiolate complexes, [Hg2(Tab)6](PF6)4.2MeCN (2.2MeCN), [Hg(Tab)2(SCN)](PF6) (3), [Hg(Tab)2(SCN)2] (4), [Hg(Tab)I2] (5), {[Hg(Tab)2]4[HgI2][Hg2I6]}(PF6)2(NO3)4 (6), [Hg(Tab)2][HgI4] (7), [Hg(Tab)2][HgCl2(SCN)2] (8), [Tab-Tab]2[Hg3Cl10] (9), and [Hg2(Tab)6]3(PF6)Cl11 (10), were prepared and characterized by elemental analysis, IR spectra, UV-vis spectra, 1H NMR, and single-crystal X-ray crystallography. The [Hg2(Tab)6]4+ tetracation of 2 or 10 contains an asymmetrical Hg2S2 rhomb with an inversion center lying on the midpoint of the Hg...Hg line. The Hg atom of the [Hg(Tab)2]2+ dication of 3 is coordinated to one SCN-, forming a rare T-shaped coordination geometry, while in 4, the Hg atom of [Hg(Tab)2]2+ is coordinated to two SCN-, forming a seesaw-shaped coordination geometry. Through weak secondary Hg...S coordinations, each cation in 3 is further linked to afford a one-dimensional zigzag chain. The trigonal [Hg(Tab)I2] molecules in 5 are held together by weak secondary Hg...I and Hg...S interactions, forming a one-dimensional chain structure. In 6, the four [Hg(Tab)2]2+ dications, one HgI2 molecule, one [Hg2I6]2- dianion, one PF6-, and four NO3- anions are interconnected by complicated secondary Hg...I and Hg...O interactions, forming a scolopendra-like chain structure. The secondary Hg...I interactions, [Hg(Tab)2]2+ and [HgI4]2- in 7, are combined to generate a one-dimensional chain structure, while [Hg(Tab)2]2+ and [HgCl2(SCN)2]2- in 8 are interconnected by secondary Hg...N interactions to form a one-dimensional zigzag chain structure. Compound 9 consists of two [Tab-Tab]2+ dications and one [Hg3Cl10]4- tetraanion. The facile approach to the construction of 2-8 and 10 from 1 may be applicable to the mimicking of a coordination sphere of the Hg sites of metallothioneins.
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PMID:Assembly of a new family of mercury(II) zwitterionic thiolate complexes from a preformed compound [Hg(Tab)2](PF6)2 [Tab = 4-(trimethylammonio)benzenethiolate]. 1652 78