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 language | English |
|---|---|
| Pages (from-to) | 161-167 |
| Number of pages | 7 |
| Journal | Journal of Biochemistry |
| Volume | 118 |
| Issue number | 1 |
| State | Published - Jul 1995 |
| Externally published | Yes |
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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 journal › Article
}
TY - JOUR
T1 - Zn2+-mediated domain-domain communication in human erythrocyte band 3
AU - Tu, Yaping
AU - Yang, F. Y.
PY - 1995/7
Y1 - 1995/7
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0028980168&partnerID=8YFLogxK
M3 - Article
VL - 118
SP - 161
EP - 167
JO - Journal of Biochemistry
JF - Journal of Biochemistry
SN - 0021-924X
IS - 1
ER -