The Binding Ability of -Lactalbumin and ß-Lactoglobulin to Mutagenic Heterocyclic Amines

¹ Department of Applied Biological Science, Hiroshima University, Higashi-Hiroshima City, Hiroshima, 724, Japan

The binding ability of bovine milk proteins with mutagenic heterocyclic amines was investigated. Binding was determined with 2 mg of ß-lactoglobulin and 20 µg of heterocyclic amine in .4 ml of pH 7.4, 50 mM phosphate buffer, at 37°C, in a shaker for 10 min. The unbound heterocyclic amine in protein-free ultrafiltrate was analyzed by HPLC method. The binding of -lactalbumin, ß-lactoglobulin A and ß-lactoglobulin B were 90.44, 81.38 and 89.18%, respectively, with 3-amino-l, 4-dimethyl-5H-pyrido[4,3-b]indole; 37.85, 34.04, and 43.90%, respectively, with 3-amino-l-methyl-5H-pyrido[4,3-b]indole; and 49.11, 43.25, and 57.44%. respectively, with 2-amino-6-methyldipyrido[1,2-a:3',2'-d] imidazole. Binding of ß-lactoglobulin and -lactalbumin to 3-amino-1,4-dimethyl-5H-pyrido[4,3-b]indole and 3-amino-1-methyl-5H-pyrido [4,3-b]-indole was higher at pH conditions above 7.4, and binding was lost at pH less than 5.5. Maximum binding of both proteins to 2-amino-6-methyl-dipyrido[1,2-a3',2'-d]imidazole was at pH 7.4, and binding was inhibited at pH conditions above 8.5 and less than 6.5.

Key Words: -lactalbumin • ßbeta;-lactoglobulin • mutagenic heterocyclic amine

Submitted on December 18, 1990
Accepted on May 31, 1991