Membrane skeletal protein structure and interactions in human erythrocytes after their treatment with diamide and calcium.

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dc.contributor.authorKumar, Jen_US
dc.contributor.authorGupta, C Men_US
dc.date.accessioned1992-04-01en_US
dc.date.accessioned2009-05-27T09:06:47Z
dc.date.available1992-04-01en_US
dc.date.available2009-05-27T09:06:47Z
dc.date.issued1992-04-01en_US
dc.description.abstractTo analyse the role of native structures of membrane proteins in their structural modifications induced by the elevated intracellular free Ca2+ levels, we have studied the Ca(2+)-mediated effects on membrane skeletal proteins in human erythrocytes that were loaded with Ca2+ using the ionophore A23187 after their pretreatment with the sulphydryl oxidizing agent, diamide. The diamide treatment not only induced polymerization of the major membrane skeletal protein, spectrin, in the erythrocytes, but it also promoted intersubunit crosslinking within the tetramers and dimers of this protein. Loading of these diamide-treated cells with Ca2+ failed to induce significant structural modifications of spectrin as well as polypeptide 4.1, another major membrane skeletal protein, as compared to the erythrocytes that were loaded with Ca2+ without the diamide pretreatment. These results have been interpreted to suggest that the Ca(2+)-induced membrane skeletal protein changes in erythrocytes depend on both the shape and relative orientation of these proteins within the membrane skeleton.en_US
dc.description.affiliationDivision of Membrane Biology, Central Drug Research Institute, Lucknow.en_US
dc.identifier.citationKumar J, Gupta CM. Membrane skeletal protein structure and interactions in human erythrocytes after their treatment with diamide and calcium. Indian Journal of Biochemistry & Biophysics. 1992 Apr; 29(2): 123-7en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/26488
dc.language.isoengen_US
dc.source.urihttps://https://www.niscair.res.in/ScienceCommunication/ResearchJournals/rejour/ijbb/ijbb0.aspen_US
dc.subject.meshActins --blooden_US
dc.subject.meshCalcimycin --pharmacologyen_US
dc.subject.meshCalcium --blooden_US
dc.subject.meshDiamide --pharmacologyen_US
dc.subject.meshErythrocyte Membrane --drug effectsen_US
dc.subject.meshErythrocytes --drug effectsen_US
dc.subject.meshHumansen_US
dc.subject.meshMacromolecular Substancesen_US
dc.subject.meshMembrane Proteins --blooden_US
dc.subject.meshSpectrin --isolation & purificationen_US
dc.titleMembrane skeletal protein structure and interactions in human erythrocytes after their treatment with diamide and calcium.en_US
dc.typeIn Vitroen_US
dc.typeJournal Articleen_US
dc.typeResearch Support, Non-U.S. Gov'ten_US
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