Document Detail


Shear-induced alignment of self-associated hemoglobin in human erythrocytes: small angle neutron scattering studies.
MedLine Citation:
PMID:  15138736     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Small angle neutron scattering (SANS) was performed on suspensions of actively metabolising human erythrocytes in the constant shear field induced by a Couette cell. The SANS pattern recorded on a two-dimensional detector was a function of the shear rate; at zero shear, the SANS pattern had radial symmetry around the direction of the beam. The radial average of the SANS pattern consisted of a broad intensity maximum superimposed on a decay. The intensity maximum at q = 0.1 A(-1) was attributed to isotropically oriented self-associated complexes of the tetrameric oxygen transport protein hemoglobin inside the erythrocytes. A flow curve of the cell suspension was used to identify at what shear rate a suspension of uniaxially oriented ellipsoidal cells is produced. The radial symmetry of the SANS patterns persisted until the shear rate was sufficient to produce a suspension of uniaxially oriented ellipsoidal cells. Again, an intensity maximum was present in directions parallel and orthogonal to the shear axis, but this intensity maximum was superimposed upon quite different intensity decays in each direction from that of the primary neutron beam. The angular range of the SANS instrument was limited, however the results from shear-induced structural changes is consistent with a model that involves hemoglobin complexes that are aligned with respect to the plasma membranes of the elongated cells.
Authors:
C J Garvey; R B Knott; E Drabarek; P W Kuchel
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2004-05-06
Journal Detail:
Title:  European biophysics journal : EBJ     Volume:  33     ISSN:  0175-7571     ISO Abbreviation:  Eur. Biophys. J.     Publication Date:  2004 Nov 
Date Detail:
Created Date:  2004-11-19     Completed Date:  2005-05-04     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  8409413     Medline TA:  Eur Biophys J     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  589-95     Citation Subset:  IM    
Affiliation:
Australian Nuclear Science and Technology Organisation, 2234 Menai, NSW, Australia. cjg@ansto.gov.au
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MeSH Terms
Descriptor/Qualifier:
Cells, Cultured
Erythrocytes / physiology*,  ultrastructure*
Hemoglobins / analysis,  metabolism*,  ultrastructure*
Humans
Mechanotransduction, Cellular / physiology*
Multiprotein Complexes / analysis,  metabolism,  ultrastructure
Protein Conformation
Shear Strength
Stress, Mechanical
Chemical
Reg. No./Substance:
0/Hemoglobins; 0/Multiprotein Complexes

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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