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Compositional Homology of Membrance-Protein Systems and Membrance-Associated Proteins: Comparaison with Milk Fat Globule Membrance and "Membrance"-Derived Xanthine Oxidease¹

Department of Food Science and Human Nutrition, Michigan State University, East Lansing 48824

ABSTRACT

Amino acid compositions of the milk fat globule membrane protein and plasma membrane protein from other sources, as well as the compositions of milk fat globule membrane-derived xanthine oxidase and selected plasma membranes-associated proteins were compared by statistical difference index. Additionally, the average hydrophobicity of xanthine oxidase and selected membrane proteins were compared. These comparisons indicate high orders of apparent compositional homology between the various plasma membranes and membrane-associated proteins. Because the biological functions of membrane proteins are widely diverse, it is speculated that their "relatedness" may reflect on evolutionary convergence to similar amino acid compositions, necessitated by their in situ environment— the lipoidal bilayer. However, compositional relatedness should not imply sequential homology.

¹ Michigan Agricultural Experiment Station Journal Article No. 7142. Partially supported by the Food and Drug Administration, Grant No. FD00567-03.

² Department of Food Science and Nutrition, Ohio State University, Columbus.