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High-affinity binding of Ca2+ to bovine α-lactalbumin in the absence and presence of EGTA

Data up to Jan 2025

Published1984
Citations27
References13

Total Citations Per Year

Abstract

References (13)

α-Lactalbumin: A calcium metalloprotein

1980 • 288 citations

Applications of Metal Buffers and Metal Indicators in Biochemistry

1956 • 158 citations

Inter- and Intramolecular Interactions of α-Lactalbumin. I. The Apparent Heterogeneity at Acid pH*

1964 • 157 citations

Characteristics of the binding of Ca2+ and other divalent metal ions to bovine alpha-lactalbumin.

1981 • 146 citations

Comparative properties of vertebrate parvalbumins.

1977 • 142 citations

Calcium binding to α-lactalbumin: Structural rearrangement and association constant evaluation by means of intrinsic protein fluorescence changes

1981 • 128 citations

Metal ion binding to .alpha.-lactalbumin species

1982 • 109 citations

Purification and properties of bovine milk glyco-α-lactalbumin

1970 • 74 citations

An experimental artifact in the use of chelating metal ion buffers. Binding of chelators to bovine alpha-lactalbumin.

1983 • 51 citations

Determination of free Ca ion concentrations with an ion-selective electrode in the presence of chelating agents in comparison with calculated values

1978 • 42 citations

Ligand binding to macromolecules: Determination of binding parameters by combined use of ligand buffers and flow dialysis; application to calcium-binding proteins

1980 • 27 citations

Investigation of the binding of Ca2+, Mg2+, Mn2+ and K+ to the vitamin D-dependent Ca2+-binding protein from pig duodenum

1984 • 21 citations

A simple procedure for purifying mammalian duodenal Ca2+-binding proteins on a 100 mg scale and an investigation of the stoichiometry of their high-affinity binding of Ca2+ ions

1983 • 14 citations

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High-affinity binding of Ca2+ to bovine α-lactalbumin in the absence and presence of EGTA (1984) – Biochemical Journal | Metascience Observatory Explorer