Stopped-flow kinetic studies of Ca(II) and Mg(II) dissociation in cod parvalbumin and bovine α-lactalbumin
- 1 December 1987
- journal article
- research article
- Published by Elsevier in Biophysical Chemistry
- Vol. 28 (3), 225-233
- https://doi.org/10.1016/0301-4622(87)80093-5
Abstract
No abstract availableThis publication has 37 references indexed in Scilit:
- Calcium release from intact calmodulin and calmodulin fragment 78–148 measured by stopped‐flow fluorescence with 2‐p‐toluidinylnaphthalene sulfonateEuropean Journal of Biochemistry, 1985
- Kinetics of calcium dissociation from calmodulin and its tryptic fragments. A stopped-flow fluorescence study using Quin 2 reveals a two-domain structureEuropean Journal of Biochemistry, 1985
- Effects of cation binding on the thermal transitions in calmodulinBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1985
- Use of lanthanide-induced nuclear magnetic resonance shifts for determination of protein structure in solution: EF calcium binding site of carp parvalbuminBiochemistry, 1983
- α-Lactalbumin binds magnesium ions: Study by means of intrinsic fluorescence techniqueBiochemical and Biophysical Research Communications, 1981
- Calcium binding to α-lactalbumin: Structural rearrangement and association constant evaluation by means of intrinsic protein fluorescence changesBiochemical and Biophysical Research Communications, 1981
- α-Lactalbumin: A calcium metalloproteinBiochemical and Biophysical Research Communications, 1980
- Calcium and magnesium binding by parvalbuminBiochimie, 1979
- A new large-scale purification procedure for muscular parvalbuminsBiochimie, 1979
- A General Strategy for Parameter Estimation from Isosteric and Allosteric‐Kinetic Data and Binding MeasurementsEuropean Journal of Biochemistry, 1972