✦ LIBER ✦

Cross-linkings between spectrin and band 3 in human erythrocyte membranes

✍ Scribed by Liu, Shih-Chun ;Palek, Jiri

Publisher: Wiley (John Wiley & Sons)
Year: 1979
Tongue: English
Weight: 849 KB
Volume: 10
Category: Article
ISSN: 0091-7419
DOI: 10.1002/jss.400100109

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✦ Synopsis

A specific structural association between spectrin component 1 and band 3 in human erythrocyte membrane has been demonstrated by covalent crosslinkings, specific labeling, and the technique of two-dimensional gel electrophoresis. A complex of 330,000 daltons, representing 1 + 3, was produced in mildly oxidized membranes at physiologic pH and isotonic conditions but not at hypotonic conditions (< 10 mM KC1 or NaCI). The yield of this complex decreased dramatically as the monovalent cation concentration decreased from 90 mM to 30 mM. The presence of Mg++ or Ca++ ( 2 mM) at low ionic strength promoted 1 + 3 cross-linking in an amount similar to that produced at isotonic conditions. The specific segment of band 3 involved in the cross-linking was also investigated by means of chymotrypsin digestion of band 3 in the intact red cells. The results showed the cross-links between spectrin component 1 and the 55,000-dalton fragment of band 3 at physiologic pH and isotonic conditions. This is consistent with the idea that band 3 is anchored o n or contacted with the submembrane meshwork at the cytoplasmic membrane surface.

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