How to Cite
Abstract
The stability of "Maize Rayado Fino Virus" capsids was studied correlating enzymatic degradation analysis of the RNA in full capsids with electron microscopy of negatively stained particles. The great thermal stability of pancreatic ribonuclease A, combined with the strong change in absorbance of the nucleic acids upon hydrolisis, provide a convenient assay for RNA release, which correlates with quantitative observations of the particles in the electron microscope. A repeatable transition between 75° and 80°C is observed with MRFV, presumably due to cooperative opening of the closed shell, followed by the release of the encapsidated RNA.References
Bloomfield, V. A., D.M. Crothers & I. Tinoco. 1974. Physical chemistry of nucleic acids. Harper & Row, Publ. Co., N. York.
Caspar, D.L.D. y A. Klug. 196 2. Physical principles in the construction of regular virus. Cold Spring Harb. Symp. Quant. Biol. 27: 1-24.
Crick, F. y J.D. Watson. 1956. Structure of small viruses. Nature 177: 73-475.
Gámez, R., T. Fukuoka, y Y. Kozuka. 1977. Purification of isometric particles from maize plants infected with rayado fino virus. Rev. Bio. Trop. 25: 151-157.
Gingery, R. E., D.T. Gordon & L.R. Nault. 1982. Purification and properties of an isolate of maize rayado fino virus from the United States. Phytopathology 72: 1313-1318.
León, P. & R. Gámez. 1986. Biología molecular del virus del rayado fino del maíz. Rev. Biol. Trop. 34: 111-114.
Mattheus, R. E. 1981. Plant Virology 2nd. edition Academic Press, N. York, pp. 858.
Comments
This work is licensed under a Creative Commons Attribution 4.0 International License.
Copyright (c) 1986 Revista de Biología Tropical