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...

Full description

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
id ftpekinguniv:oai:localhost:20.500.11897/200299
record_format openpolar
spelling ftpekinguniv:oai:localhost:20.500.11897/200299 2023-05-15T18:26:45+02:00 Characterization of hemoglobin immobilized on gamma-zirconium phosphate Geng, LN Wang, X Li, N Xiang, MH Li, KA 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. 2004 https://hdl.handle.net/20.500.11897/200299 https://doi.org/10.1016/j.colsurfb.2004.01.006 en eng colloids and surfaces b biointerfaces COLLOIDS AND SURFACES B-BIOINTERFACES.2004,34,(4),231-238. 679252 0927-7765 http://hdl.handle.net/20.500.11897/200299 doi:10.1016/j.colsurfb.2004.01.006 15261062 WOS:000220934000004 EI PubMed SCI 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 Journal 2004 ftpekinguniv https://doi.org/20.500.11897/200299 https://doi.org/10.1016/j.colsurfb.2004.01.006 2021-08-01T08:27:04Z 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 Journal/Newspaper Sperm whale Peking University Institutional Repository (PKU IR) Langmuir ENVELOPE(-67.150,-67.150,-66.967,-66.967) Colloids and Surfaces B: Biointerfaces 34 4 231 238
institution Open Polar
collection Peking University Institutional Repository (PKU IR)
op_collection_id ftpekinguniv
language English
topic 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
spellingShingle 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
Geng, LN
Wang, X
Li, N
Xiang, MH
Li, KA
Characterization of hemoglobin immobilized on gamma-zirconium phosphate
topic_facet 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
description 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
author2 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
author Geng, LN
Wang, X
Li, N
Xiang, MH
Li, KA
author_facet Geng, LN
Wang, X
Li, N
Xiang, MH
Li, KA
author_sort Geng, LN
title Characterization of hemoglobin immobilized on gamma-zirconium phosphate
title_short Characterization of hemoglobin immobilized on gamma-zirconium phosphate
title_full Characterization of hemoglobin immobilized on gamma-zirconium phosphate
title_fullStr Characterization of hemoglobin immobilized on gamma-zirconium phosphate
title_full_unstemmed Characterization of hemoglobin immobilized on gamma-zirconium phosphate
title_sort characterization of hemoglobin immobilized on gamma-zirconium phosphate
publisher colloids and surfaces b biointerfaces
publishDate 2004
url https://hdl.handle.net/20.500.11897/200299
https://doi.org/10.1016/j.colsurfb.2004.01.006
long_lat ENVELOPE(-67.150,-67.150,-66.967,-66.967)
geographic Langmuir
geographic_facet Langmuir
genre Sperm whale
genre_facet Sperm whale
op_source EI
PubMed
SCI
op_relation COLLOIDS AND SURFACES B-BIOINTERFACES.2004,34,(4),231-238.
679252
0927-7765
http://hdl.handle.net/20.500.11897/200299
doi:10.1016/j.colsurfb.2004.01.006
15261062
WOS:000220934000004
op_doi https://doi.org/20.500.11897/200299
https://doi.org/10.1016/j.colsurfb.2004.01.006
container_title Colloids and Surfaces B: Biointerfaces
container_volume 34
container_issue 4
container_start_page 231
op_container_end_page 238
_version_ 1766208729577947136

Similar Items