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...

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Bibliographic Details
Published in:Colloids and Surfaces B: Biointerfaces
Main Authors: Geng, LN, Wang, X, Li, N, Xiang, MH, Li, KA
Other Authors: Li, N (reprint author), Peking Univ, Coll Chem & Mol Engn, Minist Educ China, Key Lab Bioorgan Chem & Mol Engn, Beijing 100871, Peoples R China., Peking Univ, Coll Chem & Mol Engn, Minist Educ China, Key Lab Bioorgan Chem & Mol Engn, Beijing 100871, Peoples R China.
Format: Journal/Newspaper
Language:English
Published: colloids and surfaces b biointerfaces 2004
Subjects:
hemoglobin
gamma-zirconium phosphates
spectroscopy
isotherms
PROTEIN SECONDARY STRUCTURE
SPERM WHALE MYOGLOBIN
CIRCULAR-DICHROISM
CONFORMATIONAL-CHANGES
HORSERADISH-PEROXIDASE
ULTRAFINE PARTICLES
ENZYMATIC-ACTIVITY
ADSORPTION
INTERCALATION
DELAMINATION
Langmuir
Sperm whale
Online Access:https://hdl.handle.net/20.500.11897/200299
https://doi.org/10.1016/j.colsurfb.2004.01.006
Description
Summary: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 LIP and fitted with Langmuir and Freundlich equations. (C) 2004 Published by Elsevier B.V. Biophysics Chemistry, Physical Materials Science, Biomaterials SCI(E) EI PubMed 14 ARTICLE 4 231-238 34

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