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Science 19 April 1985:
Vol. 228. no. 4697, pp. 335 - 337
DOI: 10.1126/science.2580349
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Articles

Science, Vol 228, Issue 4697, 335-337
Copyright © 1985 by American Association for the Advancement of Science

articles

Homology of beta-lactoglobulin, serum retinol-binding protein, and protein HC

S Pervaiz and K Brew

The milk protein beta-lactoglobulin has been extensively studied but its function has not been identified. A clue regarding the function of a protein can be obtained by discovering a genetic relationship with a protein of known function through comparisons of amino acid sequence. Such comparisons revealed that beta-lactoglobulin is similar to human serum retinol-binding protein and to another human protein of unknown function known as complex-forming glycoprotein heterogeneous in charge (protein HC). beta-Lactoglobulins from several species have been found to bind retinol, while the absorption and fluorescence properties reported for the unidentified heterogeneous prosthetic group of protein HC are retinoid-like. The role of serum retinol-binding protein in vitamin A transport in the circulation suggests that the other two homologous proteins may function in the binding and transport of retinoids; beta-lactoglobulin may facilitate the absorption of vitamin A from milk and protein HC may mediate the excretion of retinol-derived metabolites.


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