Výsledky vyhledávání - "D L, Oxender"

Chemical modification of the neutral amino acid transport system L of Chinese hamster ovary cells with p-chloromercuribenzene sulfonate

Autor: G S, Campbell, J H, Yu, D L, Oxender

Publikováno v: The Journal of biological chemistry. 267(18)

Branched-chain and aromatic neutral amino acids enter mammalian cells predominantly through a Na(+)-independent transport agency called System L. The sulfhydryl specific reagent p-chloromercuribenzene sulfonate (pCMBS) has been shown to be a potent i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2c142d31c680e00ca1894612dc5d7ceb
https://pubmed.ncbi.nlm.nih.gov/1319998

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Amino acid transport in bacteria

Autor: S A, Haney, D L, Oxender

Publikováno v: International review of cytology. 137

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::1f09f824dbc0d654418523e4726e270d
https://pubmed.ncbi.nlm.nih.gov/1428673

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Altering the binding activity and specificity of the leucine binding proteins of Escherichia coli

Autor: M D, Adams, D J, Maguire, D L, Oxender

Publikováno v: The Journal of biological chemistry. 266(10)

Two leucine-binding proteins with overlapping specificities for the branched-chain amino acids are present in Escherichia coli. In order to study the basis of specificity for the very similar hydrophobic ligands, we have constructed a series of site-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2654d186963b5640053bdb5889b1e73c
https://pubmed.ncbi.nlm.nih.gov/2007577

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Second-site reversion as means of enhancing DNA-binding affinity

Autor: D L, Oxender, A L, Gibson

Publikováno v: Methods in enzymology. 208

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e177512cfac9d860624e9d86949fa47d
https://pubmed.ncbi.nlm.nih.gov/1779852

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Nucleotide sequence and genetic characterization reveal six essential genes for the LIV-I and LS transport systems of Escherichia coli

Autor: M D, Adams, L M, Wagner, T J, Graddis, R, Landick, T K, Antonucci, A L, Gibson, D L, Oxender

Publikováno v: The Journal of biological chemistry. 265(20)

The nucleotide sequence of the genes encoding the high affinity, branched-chain amino acid transport systems LIV-I and LS has been determined. Seven genes are present on a 7568-base pair DNA fragment, six of which participate directly in branched-cha

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::702449044d81e4b15b05cd40c55fd0f3
https://pubmed.ncbi.nlm.nih.gov/2195019

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Reconstitution of Neutral Amino Acid Transport Systems from Ehrlich Ascites Tumor Cells

Autor: G, Cecchini, G S, Payne, D L, Oxender

Publikováno v: Membrane Biochemistry. 1:269-278

Amino acid transport systems for alanine and leucine were reconstituted into artificial lipid vesicles. Purified plasma membrane vesicles from Ehrlich ascites cells were dissolved in 2% sodium cholate, 1mM dithiothreitol, and 0.5 mM EDTA a mixture th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6164b0f20cc06c565aedbcae7b08c8b9
https://doi.org/10.3109/09687687809063851

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The complete nucleotide sequences of the Escherichia coli LIV-BP and LS-BP genes. Implications for the mechanism of high-affinity branched-chain amino acid transport

Autor: D L Oxender, R Landick

Publikováno v: Journal of Biological Chemistry. 260:8257-8261

The Escherichia coli LIV-I and LS amino acid transport systems are high-affinity, periplasmic, binding protein-dependent systems that utilize the leucine-, isoleucine-, valine-binding protein (LIV-BP) and leucine-specific binding protein (LS-BP), res

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::3f179a937865b66e3c4f1e8befbb5990
https://doi.org/10.1016/s0021-9258(17)39464-4

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Genetic separation of high- and low-affinity transport systems for branched-chain amino acids in Escherichia coli K-12

Autor: D L Oxender, J J Anderson

Publikováno v: Journal of Bacteriology. 136:168-174

The Escherichia coli K-12 mutant strain AE4107 (livH::Mu) is defective in the high-affinity binding protein-mediated uptake system for L-leucine, L-valine, and L-isoleucine (LIV-I). We have used this strain to produce mutations in the residual LIV-II

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a2d4f04932ad105c87f04e5cbc10ed2
https://doi.org/10.1128/jb.136.1.168-174.1978

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