Stability of some Cactaceae proteins based on fluorescence, circular dichroism, and differential scanning calorimetry measurements.
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 alpha-helix.
Gorinstein
S
S
Department of Pharmaceutical Chemistry, School of Pharmacy, The Hebrew University-Hadassah Medical School, Jerusalem, Israel. gorin@cc.huji.ac.il
Zemser
M
M
Vargas-Albores
F
F
Ochoa
J L
JL
Paredes-Lopez
O
O
Scheler
C
C
Aksu
S
S
Salnikow
J
J
D002152:Calorimetry, Differential Scanning; D002942:Circular Dichroism; D015180:Electrophoresis, Gel, Two-Dimensional; D010940:Plant Proteins / Q000737:chemistry*; D010946:Plants, Medicinal / Q000737:chemistry*; D011489:Protein Denaturation; D013050:Spectrometry, Fluorescence; D017550:Spectroscopy, Fourier Transform Infrared; D013816:Thermodynamics
D010940:Plant Proteins