Abstract
Using steady-state fluorescence and nanosecond time-resolved fluorescence techniques, the Ca2+-ATPase conformational changes induced by ganglioside GM3 were studied with different quenchers. The results showed that GM3 could significantly increase the lifetime of intrinsic fluorescence of Ca2+ -ATPase reconstituted into proteoliposomes, and could also weaken the intrinsic fluorescence quenching by KI or hypocrellin B, HB. Furthermore, by using quenching kinetic analysis of the time-resolved fluorescence, in the presence of GM3, the quenching constant (Ksv) and quenching efficiency were significantly lowered. The obtained results suggest that the oligosaccharide chain and the ceramide moieties of the GM3 molecule could interact with its counterparts of the Ca2+ -ATPase respectively, thus change the conformation of the hydrophobic domain of the enzyme, making the tryptophan residues in different regions shift towards the hydrophilic-hydrophobic interface, and hence shorten the distance between the hydrophilic and the hydrophobic domains, making the enzyme with a more compact form exhibit higher enzyme activity.
| Original language | English |
|---|---|
| Pages (from-to) | 422-429 |
| Number of pages | 8 |
| Journal | Science in China, Series C: Life Sciences |
| Volume | 40 |
| Issue number | 4 |
| State | Published - 1997 |
| Externally published | Yes |
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All Science Journal Classification (ASJC) codes
- Agricultural and Biological Sciences(all)
- Agricultural and Biological Sciences (miscellaneous)
Cite this
Ganglioside GM3 modulates conformation of reconstituted Ca2+-ATPase. / Wang, Lihua; Yang, Xiaoyi; Tu, Yaping; Gui, Zhaochun; Yang, Fuyu.
In: Science in China, Series C: Life Sciences, Vol. 40, No. 4, 1997, p. 422-429.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Ganglioside GM3 modulates conformation of reconstituted Ca2+-ATPase
AU - Wang, Lihua
AU - Yang, Xiaoyi
AU - Tu, Yaping
AU - Gui, Zhaochun
AU - Yang, Fuyu
PY - 1997
Y1 - 1997
N2 - Using steady-state fluorescence and nanosecond time-resolved fluorescence techniques, the Ca2+-ATPase conformational changes induced by ganglioside GM3 were studied with different quenchers. The results showed that GM3 could significantly increase the lifetime of intrinsic fluorescence of Ca2+ -ATPase reconstituted into proteoliposomes, and could also weaken the intrinsic fluorescence quenching by KI or hypocrellin B, HB. Furthermore, by using quenching kinetic analysis of the time-resolved fluorescence, in the presence of GM3, the quenching constant (Ksv) and quenching efficiency were significantly lowered. The obtained results suggest that the oligosaccharide chain and the ceramide moieties of the GM3 molecule could interact with its counterparts of the Ca2+ -ATPase respectively, thus change the conformation of the hydrophobic domain of the enzyme, making the tryptophan residues in different regions shift towards the hydrophilic-hydrophobic interface, and hence shorten the distance between the hydrophilic and the hydrophobic domains, making the enzyme with a more compact form exhibit higher enzyme activity.
AB - Using steady-state fluorescence and nanosecond time-resolved fluorescence techniques, the Ca2+-ATPase conformational changes induced by ganglioside GM3 were studied with different quenchers. The results showed that GM3 could significantly increase the lifetime of intrinsic fluorescence of Ca2+ -ATPase reconstituted into proteoliposomes, and could also weaken the intrinsic fluorescence quenching by KI or hypocrellin B, HB. Furthermore, by using quenching kinetic analysis of the time-resolved fluorescence, in the presence of GM3, the quenching constant (Ksv) and quenching efficiency were significantly lowered. The obtained results suggest that the oligosaccharide chain and the ceramide moieties of the GM3 molecule could interact with its counterparts of the Ca2+ -ATPase respectively, thus change the conformation of the hydrophobic domain of the enzyme, making the tryptophan residues in different regions shift towards the hydrophilic-hydrophobic interface, and hence shorten the distance between the hydrophilic and the hydrophobic domains, making the enzyme with a more compact form exhibit higher enzyme activity.
UR - http://www.scopus.com/inward/record.url?scp=1542471873&partnerID=8YFLogxK
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M3 - Article
VL - 40
SP - 422
EP - 429
JO - Science in China, Series C: Life Sciences
JF - Science in China, Series C: Life Sciences
SN - 1006-9305
IS - 4
ER -