TY - JOUR
T1 - Stability of some cactaceae proteins based on fluorescence, circular dichroism, and differential scanning calorimetry measurements
AU - Gorinstein, Shela
AU - Zemser, Marina
AU - Vargas-Albores, Francisco
AU - Ochoa, Jose Luis
AU - Paredes-Lopez, Octavio
AU - Scheler, Christian
AU - Aksu, Sevil
AU - Salnikow, Johann
PY - 1999
Y1 - 1999
N2 - 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 α-helix.
AB - 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 α-helix.
KW - Cactaceae
KW - Calorimetry
KW - Denaturation
KW - Electrophoresis
KW - Fluorescence
KW - Proteins
KW - Spec troscopy
UR - http://www.scopus.com/inward/record.url?scp=53149132780&partnerID=8YFLogxK
U2 - 10.1023/A:1020640409179
DO - 10.1023/A:1020640409179
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C2 - 10333299
AN - SCOPUS:53149132780
SN - 0277-8033
VL - 18
SP - 239
EP - 247
JO - Journal of Protein Chemistry
JF - Journal of Protein Chemistry
IS - 2
ER -