| Issue |
J. Phys. Colloques
Volume 48, Number C7, Décembre 1987
1st International Laser M2P Conference
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|---|---|---|
| Page(s) | C7-625 - C7-627 | |
| DOI | https://doi.org/10.1051/jphyscol:19877151 | |
J. Phys. Colloques 48 (1987) C7-625-C7-627
DOI: 10.1051/jphyscol:19877151
PROBING THE METAL BINDING SITES OF α-LACTALBUMIN WITH LASER-EXCITED Eu(III) IONS
J.-C.G. BÜNZLI, P.D. MORAND and J.-M. PFEFFERLÉInstitut de Chimie Minérale et Analytique, Université de Lausanne, Place du Château 3, CH-1005 Lausanne, Switzerland
Abstract
α-lactalbumin, also known as the B-protein of the lactose synthetase enzymatic complex, is a soluble milk protein which is secreted throughout lactation and functions as an "on-off" switch in the synthesis of lactose. The protein has a molecular weight of 14,200 and contains 123 amino acid residues arranged in a sequence similar to that of egg-white lysozyme [1]. The protein in its native form contains one or two Ca(II) ions per mole but despite extensive investigation, mainly by Kronman and coworkers [2,3,4,8], the number and location of the sites for attachment of calcium remain ill-defined. We have initiated a study to determine further the number and nature of the protein metallic sites using Eu(III) as a luminescent binding probe.