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Recubrimiento de quitosán en aguacate 23 6. Biale, J.B.; Young, R.E., The avocado pear. En: Hulme A.C. (Ed.). The biochemistry of fruits and their products. (1971) Vol. 2 London Academic Press,. pp. 2-63. 7. Rodríguez Suppo, F., El aguacate. De AG editor S.A. México. 1982, pp. 16-21, 45-53, 141. 8. Wills, R.H.H.; Lee, T.H.; Mc Glasson, W.B.; Hall, E.G.; Graham D. Fisiología y Manipulación de Frutas y Hortalizas Post-Recolección. Edit. Acribia, pp. 18-27, 37-41, 58-67. 9. Yahia, E.M.; Higuera, C.I. Fisiología y Tecnología de productos hortícolas, Ed. Limusa 1992, pp. 21-23, 201-205. 10. Yahia, E.M. Horticultura Internacional 1995, 7 y 8, pp 37-39, 20- 25. 11. Yahia, E.M. Centro de Investigación en Alimentación y Desarrollo, A.C., Apartado Postal 1735, Hermosillo, Sonora, 83000, México. 12. Knorr, D. Food Technol. 1991, 114-121. 13. Muzzarelli, R.A.A., Chitin, Japan Seminary on Advances in chitin, chitosan and Related Enzymes, Pergamon Press, 1977, Fifth edition, pp. 30-44. 14. El Graouth, A.; Arul, J.; Ponnampalom, R.; Boulet, M., J. Food. Sci., 1991, 56, 1618-1631. 15. El Graouth, A.; Ponnampalom, R.; Castaige, F.; Arul, J. Hort. Sci., 1992, 27, 1016-1017. 16. El Graouth, A.; Arul, J.; Grenier, J.; Asselin, A. Phytopathology, 1992, 82, 398-402. 17. Wong, D.W.S.; Gastineau, F.A.; Gregorski, K.S.; Tillin, Sandra J.; Pavlath, Attila E. J. Agric. Food Chem. 1992,40, 540-544. 18. Vojdani F.; Torres J.A. J. Food Sci. 1990, 55, 841-846. 19. Lazaro B.V., “Incidencia de Antracnosis en Aguacate Variedad Hass” Tesis, 1985 FES-C, UNAM, pp. 26-29. 20. Queralt, G.E. El cultivo moderno del aguacate. 1987. Ed. De Vecchi, S.A. Barcelona, pp. 114. 21. Streets, R. B. The diagnosis of plant diseases. 1975. A field and laboratory manual emphasizing the most practical methods for rapid identification. The University of Arizona Press. fourth printing, pp. 7.13, 7.14. 22. Alimentaria Mexicana Bekarem, S.A. DE C.V. Carrion y Rubio No. 21 Sta. Martha Acatitla, C.P. 09510, México D.F. 23. García-Tinajero, R.; Córdoba-Ponce, R. Manual Ilustrado de técnicas de laboratorio utilizadas en bacteriología y micología veterinarias de SARH, 1988, pp. 257-262. 24. Introducción a la Micología Industrial George Smith Zaragoza España Ed. Acribia, pp. 332-337. 25. Méndez Posadas A.; Mundo E.; Marín S. T. Monografías UNAM. Análisis de experimentos con observaciones repetidas. Instituto de Investigaciones Aplicadas y en Sistemas. Vol. 4, No. 3, 1994, pp. 1-21.
Revista de la Sociedad Química de México, Vol. 43, Núm. 1 (1999) 24-29 Revisión An Integrated, Holistic Experimental and Theoretical Approach Applied to the Derivation of the 3D Structure of Bovine Amelogenin implicated in Amelogenesis imperfecta, a Molecular Disease Characterized by a Single Point Mutation V. Renugopalakrishnan l, 2 *, R. Garduño-Juárez 3 , Juan Carlos Hernández Guerrero 4 , Patricia N. Casillas Lavín 4 and K. Ilangovan 5 1 Harvard Medical School, Harvard University, 423 Av., Boston, MA 02115, USA, Fax +1.617.738.4960; 2 Instituto de Química, Universidad Nacional Autónoma de México, Circuito Exterior, Ciudad Universitaria, Coyoacán, 04510 México DF, México. Fax +52-5616-2217, email: renu@servidor.unam.mx; 3 Centro de Ciencias Físicas, Universidad Nacional Autónoma de México, 62210 Cuernavaca, Morelos, México; 4 Facultad de Odontología, Universidad Nacional Autónoma de México, 04510 México DF, México; 5 Instituto de Ingeniería, Universidad Nacional Autónoma de México, 04510 México DF, México. Resumen. La amelogenina, una fosfoproteína de 170 residuos, de ~19kDa, extracelular e hidrofóbica, con una estructura elipsoidal, secretada por los ameloblastes dentales bovinos, contiene una estructura primaria única comparada con otras proteínas de mamíferos de estructura primaria conocida. Se caracteriza por una proporción alta de Leu, His, Met, Gln, y Pro, y también contiene un residuo de Ser 16 fosforilado. Se revisan los estudios de ingeniería genética combinados con investigación en biología estructural. La estructura tridimensional de la amelogenina dental de bovinos ha sido el tema de investigación del autor principal en la Escuela Médica de Harvard desde 1984, empleando aproximaciones teóricas y experimentales integradas. Estas aproximaciones se describen mediante un diagrama de flujo. Su estructura tridimensional contiene numerosos giros β-, una estructura espiral β-, segmentos de hojas β-aislados, y tiene un contenido bajo α-helicoidal. Los mutantes de la amelogenina y algunos fragmentos sintéticos tienen potencial clínico en el tratamiento de la Amelogenesis imperfecta, una enfermedad dental prevalente en México. Palabras clave: RMN 3D, IR-TF, Raman, DC, Flourescencia, Síntesis de polipéptidos, Enfermedad molecular, Dinámica molecular, Canal de iones, M179 resíduo recombinante, amelogenina, estructura secundaria. Introduction Abstract. Bovine Amelogenin, a 170-residue, ~19 kDa extracellular, hydrophobic, phosphoprotein with an overall ellipsoidal shape, secreted by ameloblasts from bovine tooth enamel, contains a primary structure which is unique in comparison to other known primary structures of mammalian proteins. lt is characterized by a large proportion of Leu, His, Met, Gln, and Pro residues and also contains a single phosphorylated Ser16 residue. Genetic engineering studies combined with structural biological research are discussed in this review. 3D structure of bovine tooth amelogenin has been the focus of research by the principal author at Harvard Medical School since 1984 using an integrated experimental and theoretical approach. A flow sheet describes the general strategy for such an integrated approach. Its 3D structure contains numerous β-turns, a β-spiral structure, isolated β-sheet segments, and is low in α-helical content. Amelogenin mutants and synthetic fragments have potencial clinical use in fighting amelogenesis imperfecta, a dental disease which is prevalent in Mexico. Key Words: 3D NMR, FT-IR, Raman, CD, Time-resolved Fluorescence, Polypeptide synthesis, Molecular Disease, Molecular Dynamics, Ion Channel, Ml79-a 179 residue recombinant mouse amelogenin, Secondary Structure. Structural biology of proteins has made significant advances in the last two decades, propelled by multi-nuclear 2D and 3D NMR spectroscopy [l], X-ray and Neutron diffraction Fourier transform infrared (FT-IR) [2], laser Raman spectroscopy (LRS), small angle neutron scattering.(SANS), time-resolved flurorescence spectroscopy, molecular mechanics-dynamics approach [3], solid-phase peptide synthesis and the capability to produce monoclonally pure proteins by expression of appropriate cDNA’s in a bacterial cell e.g. E. coli and site-specific mutagenesis to synthesize mutant proteins. Structural biology and molecular biology have therefore become interdependent. Despite all these impressive technical developments, the solution-phase structure of proteins with M r > 30 kDa by heteronuclear multi-dimensional NMR [1] continues to pose formidable challenges especially in the assignment of proton resonances. FT-IR and LRS have no limitations on the M r of proteins which can be investigated using these two methods. The development of 2D Heterospectral IR-Raman [4], is a significant advance of immense value to protein structural biology. In terms of the structural information content, NMR spectroscopy rivals with X-ray and neutron diffraction. In the case of membrane proteins and proteins that are stubborn to crystallization due to their mobility of the glycosamino glycan (GAG) and lipid side chains [1] e.g. glycoproteins, pro-
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