Zobrazeno 1 - 10
of 12
pro vyhledávání: '"William A. Strycharz"'
Publikováno v:
European Journal of Biochemistry. 48:303-310
1 An IF-M3-deficient ascites cell-free system is described. 2 An IF-M3 species of high molecular weight has been isolated and partially purified from a high-KCl ascites ribosomal wash fluid. 3 Translation of encephalomyocarditis virus RNA and globin
Publikováno v:
Journal of Molecular Biology. 126:123-140
Ribosomal proteins L 7 L 12 have been mapped by immune electron microscopy. These multiple copy proteins are located at a single region extending from the large subunit, known as the L 7 L 12 stalk. The L 7 L 12 stalk is approximately 100 A long, abo
Autor:
Thomas R. Tritton, William A. Strycharz, Barry S. Cooperman, Robert A. Goldman, Bruce A. Williams
Publikováno v:
FEBS Letters. 118:113-118
The E. colt’ ribosome is currently the object of a great variety of studies which seek to define its function in terms of its structure. Photoaffinity labeling has proven to be a valuable tool in this regard [ 11. We are currently using this techni
Publikováno v:
Journal of Molecular Biology. 152:397-412
Three forms of the 50 S ribosomal subunit of Escherichia coli have been separated by agarose/acrylamide gel electrophoresis. The slowest migrating form, S-50 S, corresponded to native 50 S subunits and contained four copies of proteins L 7 L 12 . Rem
Autor:
James A. Lake, William A. Strycharz
Publikováno v:
Journal of molecular biology. 153(4)
Three-dimensional locations have been determined for Escherichia coli ribosomal proteins L1, L17 and L27 by immune electron microscopy using antibodies directed against these proteins. From the positions of immunoglobulin G attachment, observed in tw
Autor:
Dipak B. Datta, Li-Ming Changchien, Gary R. Craven, William A. Strycharz, Concepcion R. Nierras
Publikováno v:
Analytical biochemistry. 173(2)
We have developed a two-dimensional gel electrophoretic system for the identification of Escherichia coli ribosomal proteins that involves the use of acid-urea in the first dimension and sodium dodecyl sulfate in the second dimension. This system has
Publikováno v:
Biochemistry. 22(6)
Translation initiation factor 3 (IF-3) was bound noncovalently to Escherichia coli 50S ribosomal subunits. Irradiation of such complexes with near-ultraviolet light (greater than 285 nm) resulted in covalent attachment of initiation factor 3 to the 5
Publikováno v:
Biochemistry. 22(2)
Autor:
Leonard E. Post, Lasse Lindahl, Scott F. Gilbert, Janice M. Zengel, William A. Strycharz, Masayasu Nomura
hfus3 (or hfus2) transducing phage stimulates the synthesis of 27 ribosomal proteins, elongation factors EF-Tu and EF-G, and RNA polymerase subunit (Y in ultraviolet-irradiated Escherichia roli cells (see a preceding paper, Jaskunas, S. R., Fallon, A
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a836781bf110349d3d991bd0d41218e
Publikováno v:
Biochemistry. 21(16)
The photoincorporation of p-azido[3H]puromycin [6-(dimethylamino)-9-[3'-deoxy-3'-[(p-azido-L-phenylalanyl)amino]-beta-D-ribofuranosyl]purine] into specific ribosomal proteins and ribosomal RNA [Nicholson, A. W., Hall, C. C., Strycharz, W. A., & Coope