In:
FEBS Letters, Wiley, Vol. 277, No. 1-2 ( 1990-12-17), p. 147-150
Abstract:
Fourier transform infrared spectroscopy was used to study ligand binding and conformational changes in the Ca 2+ ‐ATPase of sarcoplasmic reticulum. Novel in infrared difference spectroscopy, the catalytic cycle in the IR sample was started by photolytic release of ATP from an inactive, photolabile ATP‐derivative (caged ATP). Small, but characteristic infrared absorbance changes were observed upon ATP release. On the basis of model spectra, the absorbance changes corresponding to the trigger and substrate reactions, i.e. to photolysis of caged ATP and hydrolysis of ATP, were separated from the absorbance changes due to the active ATPase reflecting formation of the phosphorylated Ca 2 E 1 P enzyme form. A major rearrangement of ATPase conformation as the result of catalysis can be excluded.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(90)80830-C
Language:
English
Publisher:
Wiley
Publication Date:
1990
detail.hit.zdb_id:
1460391-3
SSG:
12
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