Results 251 to 260 of about 80,417 (311)
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Interaction of tobacco mosaic virus and tobacco mosaic virus protein with bovine serum albumin

Archives of Biochemistry and Biophysics, 1977
Abstract Bovine serum albumin (BSA) causes tobacco mosaic virus (TMV) to crystallize at pH values where both have negative charges. The amount of albumin required to precipitate the virus varies inversely with ionic strength of added electrolyte. At pH values above 5, the precipitating power is greatest when BSA has the maximum total, positive plus ...
Max A. Lauffer, Ragaa A. Shalaby
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Distribution of Radiocarbon in Tobacco Mosaic Virus

Nature, 1955
WE have made radioactive tobacco mosaic virus by exposing leaves from infected tobacco plants to radioactive carbon dioxide for one day in light, treating the homogenized leaves with buffer solution, and purifying the virus by repeated precipitation at the isoelectric point1.
Wüstinger, G.   +2 more
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Structure of the Tobacco Mosaic Virus Particle; Polymerization of Tobacco

1968
Publisher Summary The chapter describes a critical analysis of the molecular weight of tobacco mosaic virus (TMV) and with polymerization of TMV protein. TMV has a very high molecular weight and measurements of double refraction of flow led to the conclusion that the particles are rod-shaped. The molecular weight of TMV has been determined adequately
Max A. Lauffer, Charles L. Stevens
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Fine Structure of Tobacco Mosaic Virus

Nature, 1956
ALTHOUGH tobacco mosaic was one of the first viruses to be examined in the electron microscope, electron microscopy has failed to reveal any fine structure, even though it has been repeatedly looked for1,2, especially since the introduction3 of metal shadow casting in 1945.
Richard F. Baker, Richard F. Baker
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ZONE ELECTROPHORESIS OF TOBACCO MOSAIC VIRUS

Canadian Journal of Biochemistry and Physiology, 1959
An apparatus is described for the preparative zone electrophoresis of tobacco mosaic virus in agar gel. The isolated virus does not have any detectable ribonuclease activity.
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Partial reconstitution of tobacco mosaic virus

Virology, 1969
Abstract TMV reconstitutes rapidly in vitro at 24°; a yield of 30% was obtained after 30 min of reconstitution. The maximum yield was around 60%, reached after 7 hours. Electron micrographs of reconstituted TMV suspensions show particles of predominant lengths 700 A and 3000 A.
L. Hirth, G. Lebeurier, C. Stussi
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Cation binding by tobacco mosaic virus

Virology, 1977
Abstract Hydrogen ion titration curves of tobacco mosaic virus and its protein, alone or in the presence of various multivalent ions, have been measured. Three groups titrating near neutral pH in the virion have significant metal ion binding, but the tightest of these binding sites, significantly specific for Ca 2+ over Mg 2+ appears to be absent ...
Donald A. Hendry, Anthony C.H. Durham
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Flexibility in tobacco mosaic virus.

Ciba Foundation symposium, 1983
Tobacco mosaic virus (TMV) particles are rod-like, 300 nm long and 18 nm in diameter. TMV consists of 2140 protein subunits, each with a relative molecular mass of 17420 (158 residues), arranged on a helix of pitch 2.3 nm with 16 1/3 subunits per turn. Winding through this helix is a single strand of RNA 6400 nucleotides long.
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Structural Aspects of Tobacco Mosaic Virus

1959
Publisher Summary This chapter aims to summarize the currently prevailing concepts concerning chemical structure and biological function of the tobacco mosaic virus particle, quoting in many instances only the last stepping stones toward present position. Most of the emphasis is on the protein, concerning the structure and function of which have more
H. Fraenkel-Conrat, L.K. Ramachandran
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