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This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Allen, D. W. Articles by White, J. G. Search for Related Content PubMed PubMed Citation Articles by Allen, D. W. Articles by White, J. G. Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Comparison of hemoglobin Koln erythrocyte membranes with malondialdehyde-reacted normal erythrocyte membranes DW Allen, CF Burgoyne, JD Groat, CM Smith and JG White Splenectomized patients with hemoglobin (Hb) Koln have rigid RBCs with membrane polypeptide aggregates that are not dissociable with disulfide- reducing agents. Malondialdehyde (MDA) action on normal RBCs produced rigid RBCs with similar nondissociable aggregates. To test the hypothesis that Hb Koln RBC aggregates contained unsaturated MDA-type bonds, we reduced normal control RBC membranes, Hb Koln RBC membranes, and MDA-reacted membranes with [3H]NaBH4. Hb Koln RBC membranes and MDA- reacted membranes both had significantly more 3H incorporation than control membranes. Furthermore, 3H incorporation in both Hb Koln and MDA-treated membranes was located in the membrane polypeptide aggregates, presumably saturating the crosslinking bonds. After reaction of RBCs with [14C]MDA, the MDA label was similarly concentrated in the membrane polypeptide aggregates. Normal RBC membranes incubated with MDA were analyzed with and without reduction by NaBH4 prior to amino acid determination by high-performance liquid chromatography (HPLC). Reduction with NaBH4 after MDA treatment decreased the lysyl residues by 33% and the serine by 7% and increased by 10% the methionyl residues, but did not affect 12 other amino acids. Similar changes could be detected in NaBH4-reduced Hb Koln aggregates in methionine and serine content. MDA may also alter protein configuration, as evidenced by an increase in the protease susceptibility of membrane proteins from MDA-treated and Hb Koln RBCs. We conclude that Hb Koln RBC membranes, like MDA-treated membranes, have similar high molecular weight aggregates conferring decreased membrane deformability, [3H]NaBH4-reducible unsaturated bonds, changes in amino acid composition upon reduction, and protease-sensitive configurational changes. Volume 64, Issue 6, pp. 1263-1269, 12/01/1984 Copyright © 1984 by The American Society of Hematology CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

	Copyright © 1984 by American Society of Hematology         Online ISSN: 1528-0020