Characterization of hemoglobin immobilized on gamma-zirconium phosphate.
The fact that different gamma-zirconium phosphate (gamma-ZrP) preintercalation method induced varied degree and type of conformational change of the adsorption protein was confirmed by characterization techniques including circular dichroism (CD), fourier transform infrared spectroscopy (FTIR) and X-ray powder diffraction (XRD) analysis. The results indicated that the association of hemoglobin with gamma-ZrP preintercalated using butylamine was correlated with conformational change in the secondary structure of the protein. gamma-ZrP which was preintercalated with tetra (n-butylammonium) hydroxide caused the conformational change of Hemoglobin in both the secondary structure and the tertiary structure. X-ray powder diffraction analysis was used to analyze the crystalline structure of the nanocomposites prepared by relamination. The adsorption isotherms of Hemoglobin on different matrices were set up and fitted with Langmuir and Freundlich equations.
Geng
LiNa
L
Key Laboratory of Bioorganic Chemistry and Molecular Engineering of Ministry of Education of China, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, People's Republic of China.
Wang
Xu
X
Li
Na
N
Xiang
MingHui
M
Li
Ke'an
K
D000042:Absorption; D002942:Circular Dichroism; D006454:Hemoglobins / Q000737:chemistry*; D011208:Powders; D011487:Protein Conformation; D000644:Quaternary Ammonium Compounds / Q000737:chemistry; D017550:Spectroscopy, Fourier Transform Infrared; D014961:X-Ray Diffraction; D015040:Zirconium / Q000737:chemistry
D006454:Hemoglobins; D011208:Powders; D000644:Quaternary Ammonium Compounds; C027006:zirconium phosphate; D015040:Zirconium; C009405:tetrabutylammonium