Zobrazeno 1 - 10
of 41
pro vyhledávání: '"D L Oxender"'
Publikováno v:
Current opinion in biotechnology. 4(6)
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
Autor:
S A, Haney, D L, Oxender
Publikováno v:
International review of cytology. 137
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-
Autor:
D L, Oxender, A L, Gibson
Publikováno v:
Methods in enzymology. 208
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
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
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
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
Publikováno v:
Diabetes. 29:317-322