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Vitamin C transport systems of mammalian cells
TLDR
Two isoforms of vitamin C transport proteins, SVCT1 and SVCT2, have recently been cloned from humans and rats and are predicted to have 12 transmembrane domains, but they share no structural homology with other Na+ co-transporters.
Cation and sugar selectivity determinants in a novel family of transport proteins
TLDR
A new family of homologous membrane proteins that transport galactosides–pentoses–hexuronides (GPH) is described and it is speculated on the cation binding pocket of this family of transporters.
Unidirectional Reconstitution into Detergent-destabilized Liposomes of the Purified Lactose Transport System of Streptococcus thermophilus*
TLDR
Under these conditions proteoliposomes were obtained in which LacS was reconstituted in an inside-out orientation, as suggested by the outside labeling of a single cysteine mutant with a membrane impermeable biotin-maleimide.
Purification and reconstitution of an osmosensor: transporter ProP of Escherichia coli senses and responds to osmotic shifts.
TLDR
Pure ProP acts, in the proteoliposome environment, as sensor, transducer, and respondent to a hyperosmotic shift, and is the first such osmosensor to be isolated.
Regulation of the human vitamin C transporters expressed in COS-1 cells by protein kinase C [corrected].
TLDR
Western blot and confocal microscopy analyses indicated that the total pool of hSVCT1 or hSvCT2 proteins expressed in the transfected COS-1 cells remained unaffected by PMA treatment, suggesting that the PKC-dependent modulation of L-ascorbic acid transport mediated by hVCT2 was the result of reduced catalytic transport efficiency.
Laboratory and field validation of a simple method for detecting four species of non-native freshwater fish using eDNA.
TLDR
The filtration of small volumes of pond water was sufficient to capture fish eDNA and the approach emphasised the importance of taking multiple water samples of sufficient spatial coverage for detecting species of random or patchy distribution.
Sugar-cation symport systems in bacteria.
The gusBC Genes of Escherichia coli Encode a Glucuronide Transport System
TLDR
Two genes, gusB and gusC, from a natural fecal isolate of Escherichia coli are shown to encode proteins responsible for transport of beta-glucuronides with synthetic [(14)C]phenyl-1-thio-beta-d- glucuronide as the substrate, which showed that it is essential for glucuronide transport and is located in the inner membrane.
Expression of prokaryotic membrane transport proteins in Escherichia coli.
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