Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Ravi Kambampati"'
Autor:
Susan Peng, Nancy M. Dahms, Ravi Kambampati, Xu Wang, Jonathan H. LeBowitz, Peggy Tom, John Maga, Richard N. Bohnsack, Jianghong Zhou, Angela M. Thomm, Barry J. Byrne, Sarah Golata
Publikováno v:
The Journal of Biological Chemistry
Background: Acid α-glucosidase, an enzyme replacement therapy for Pompe disease, is poorly targeted to lysosomes when relying on phosphomannose residues. Results: Fusing IGF-II to acid α-glucosidase resulted in more efficient uptake and glycogen cl
Publikováno v:
Cornea. 26:1213-1219
PURPOSE To determine matrix metalloproteinase (MMP) 2 and MMP 9 expression in acute and chronic experimentally wounded canine corneas and keratectomy samples from canine patients with spontaneous chronic corneal epithelial defects (SCCEDs). METHODS M
Autor:
Ravi Kambampati, Charles T. Lauhon
Publikováno v:
Biochemistry. 42:1109-1117
Thionucleosides are uniquely present in tRNA. In many organisms, tRNA specific for Lys, Glu, and Gln contain hypermodified 2-thiouridine (s2U) derivatives at wobble position 34. The s2 group of s2U34 stabilizes anticodon structure, confers ribosome b
Autor:
Anthony A. Paiva, Lee Huang, Liane M. Mende-Mueller, Ravi Kambampati, Carla B. Pellegrino, Kalpana Chakraburtty
Publikováno v:
Journal of Biological Chemistry. 275:16963-16968
Elongation factor 3 (EF-3) is an ATPase essential for polypeptide chain synthesis in a variety of yeasts and fungi. We used limited proteolysis to study the organization of the subdomains of EF-3. Trypsinolysis of EF-3 at 30 °C resulted in the forma
Autor:
Ravi Kambampati, Charles T. Lauhon
Publikováno v:
Journal of Biological Chemistry. 275:10727-10730
IscS from Escherichia coli is a cysteine desulfurase that has been shown to be involved in Fe-S cluster formation. The enzyme converts L-cysteine to L-alanine and sulfane sulfur (S(0)) in the form of a cysteine persulfide in its active site. Recently
Autor:
Ravi Kambampati, Charles T. Lauhon
Publikováno v:
Biochemistry. 38:16561-16568
We have improved the in vitro assay for 4-thiouridine (s(4)U) biosynthesis in Escherichia coli tRNA by substituting an unmodified tRNA transcript as substrate and including recombinant ThiI protein, a known factor required for s(4)U synthesis. Using
Publikováno v:
European Journal of Biochemistry. 258:986-993
Elongation factor 3 (EF-3) is an essential requirement for translation in fungi. We previously reported activation of EF-3-ATPase by yeast ribosomes. EF-3 interacts with both ribosomal subunits and shows high affinity for 60S subparticles. Translatio
Autor:
Ravi Kambampati, Kalpana Chakraburtty
Publikováno v:
Journal of Biological Chemistry. 272:6377-6381
Elongation factor 3 (EF-3) is an essential requirement of the fungi for translational elongation. EF-3 is an ATPase, and the hydrolytic activity is stimulated 2 orders of magnitude by yeast ribosomes. Limited trypsinolysis of EF-3 results in the clea
Autor:
Ravi, Kambampati, Charles T, Lauhon
Publikováno v:
Biochemistry. 42(4)
Thionucleosides are uniquely present in tRNA. In many organisms, tRNA specific for Lys, Glu, and Gln contain hypermodified 2-thiouridine (s(2)U) derivatives at wobble position 34. The s(2) group of s(2)U34 stabilizes anticodon structure, confers ribo
Autor:
Ravi Kambampati, Kalpana Chakraburtty
Publikováno v:
Protein expression and purification. 10(2)
The translational elongation factor 3 (EF-3) from Saccharomyces cerevisiae was overexpressed and purified to near homogeneity from the post-ribosomal supernatant fraction (S-100). A detailed protocol for the isolation of overexpressed EF-3 is present