@article{oai:ir.soken.ac.jp:00004146,
 author = {桑島, 邦博 and PERMYAKOV, Eugene A and GRISHCHENKO, Valery M and KALINICHENKO, Lina P and ORLOV, Nikolay Y and KUWAJIMA, Kunihiro and SUGAI, Shintaro},
 issue = {2},
 journal = {Biophysical Chemistry, Biophysical Chemistry},
 month = {Feb},
 note = {Affinity chromatography, fluorescence and circular dichroism spectroscopy methods have been used to study the interaction of melittin, a 26-residue peptide from bee venom, with Ca2+-binding α-lactalbumin from human milk. It has been revealed that melittin binds to the apo- and acidic states of α-lactalbumin while the presence of Ca2+ makes the interaction essentially weaker. The association constant for the complex of melittin with apo-α-lactalbumin determined from spectropolarimetric melittin-titration data is 2×107 M−1. The complexation of α-lactalbumin with melittin decreases its affinity to Ca2+ by three orders of magnitude. The interaction of apo-α-lactalbumin with melittin causes some changes in the environment of its aromatic amino acid residues and drastically alters the conformation of melittin, increasing its α-helical content but leaving its single tryptophan residue accessible to water. In the case of the acidic state of α-lactalbumin the interaction does not induce an increase in α-helical content of melittin.},
 pages = {111--117},
 title = {Calcium-regulated interactions of human α-lactalbumin with bee venom melittin},
 volume = {39},
 year = {1991}
}