Stability of Some Cactaceae Proteins Based on Fluorescence, Circular Dichroism, and Differential Scanning Calorimetry Measurements |
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Authors: | Shela Gorinstein Marina Zemser Francisco Vargas-Albores Jose-Luis Ochoa Octavio Paredes-Lopez Christian Scheler Sevil Aksu Johann Salnikow |
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Affiliation: | (1) Department of Pharmaceutical Chemistry, School of Pharmacy, The Hebrew University-Hadassah Medical School, P.O.B. 12065, Jerusalem, 91120, Israel;(2) Division de Biologia Experimental, Centro de Investigaciones Biologicas del Noroeste SC, P.O. Box 128, La Paz, Baja California Sur, 23000, Mexico;(3) Departamento de Biotecnologia y Bioquimica, Centro de Investigacion y de Estudios Avanzados del IPN, Unidad Irapuato, Apdo. Postal 629, 36500 Irapuato, Gto, Mexico;(4) Wittman Institute of Technology and Analysis of Biomolecules, Teltow, Germany;(5) Institut für Biochemie und Molekulare Biologie, Technische Universitat Berlin, Berlin, Germany;(6) Affiliated with the David R. Bloom Center for Pharmacy, Jerusalem, Israel |
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Abstract: | Characterization of three cactus proteins (native and denatured) from Machaerocereus gummosus (Pitahaya agria), Lophocereu schottii (Garambullo), and Cholla opuntia (Cholla), was based on electrophoretic, fluorescence, CD (circular dichroism), DSC (differential scanning calorimetry), and FT-IR (Fourier transform infrared) measurements. The obtained results of intrinsic fluorescence, DSC, and CD were dissimilar for the three species of cactus, providing evidence of differences in secondary and tertiary structures. Cactus proteins may be situated in the following order corresponding to their relative stability: Machaerocereus gummosus (Pitahaya agria) > Cholla opuntia (Cholla) > Lophocereu schottii (Garambullo). Thermodynamic properties of proteins and their changes upon denaturation (temperature of denaturation, enthalphy, and the number of ruptured hydrogen bonds) were correlated with the secondary structure of proteins and disappearance of -helix. |
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Keywords: | Cactaceae proteins electrophoresis fluorescence calorimetry denaturation spectroscopy |
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