Zn2+-mediated domain-domain communication in human erythrocyte band 3

Yaping Tu, F. Y. Yang

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Zn2+ could inhibit the anion transport activity of spectrin-stripped inside-out human erythrocyte membrane vesicles (IOVs). Removal of the cytoplasmic domain from Band 3 by trypsin could eliminate Zn2+ inhibition. The location of a Zn2+-binding site was confirmed by atomic absorbance spectrometry. The results of time-resolved fluorescence and intrinsic fluorescence quenching by KI and hypocrellin B (a photosensitive pigment obtained from a parasitic fungus growing in Yunnan, China) showed that the cytoplasmic domain is necessary for the Zn2+-induced conformational changes of the whole molecule as well as the membrane domain of Band 3. It is suggested that Zn2+ induced a conformational change in the cytoplasmic domain of Band 3, which in turn was transmitted to the membrane domain, resulting in an inhibition of activity of Band 3. Such long-range conformational changes may imply that the cytoplasmic domain is poised to function as a cytosolic arm in order to modulate the structure of the membrane domain of Band 3.

Original languageEnglish
Pages (from-to)161-167
Number of pages7
JournalJournal of Biochemistry
Volume118
Issue number1
StatePublished - Jul 1995
Externally publishedYes

Fingerprint

Erythrocyte
Erythrocytes
Communication
Membranes
Fluorescence
Membrane
Spectrin
Erythrocyte Membrane
Trypsin
Anions
China
Spectrum Analysis
Fungi
Binding sites
Binding Sites
Pigments
Spectrometry
Quenching
Negative ions
Vesicles

All Science Journal Classification (ASJC) codes

  • Statistics, Probability and Uncertainty
  • Applied Mathematics
  • Physiology (medical)
  • Radiology Nuclear Medicine and imaging
  • Molecular Biology
  • Biochemistry

Cite this

Zn2+-mediated domain-domain communication in human erythrocyte band 3. / Tu, Yaping; Yang, F. Y.

In: Journal of Biochemistry, Vol. 118, No. 1, 07.1995, p. 161-167.

Research output: Contribution to journalArticle

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