Components of the major urinary protein complex in inbred mice: separation and peptide mapping.

Abstract

Gel filtration of the nondialyzable fraction of urine from normal inbred mice on Sephadex G-100 yielded three peaks (I, II, and III in order of elution), the relative sizes of which varied with the sex and strain of the mice. Constituents of peak I, the breakthrough peak, included uromucoid (Tamm-Horsfall mucoprotein); peak III was low in nitrogen, rich in carbohydrate, nonprecipitable with trichloroacetic acid, gave no definitive ultraviolet or visible spectrum, and had a sedimentation coefficient of 0.5 S. Peak II contained the electrophoretically distinguishable prealbumins of the major urinary protein (MUP) complex. These components (known as 1, 2, and 3 in order of increasing mobility toward the anode) were separated by chromatography on diethylaminoethyl cellulose. Tryptic peptide mapping indicated that components 1 and 2, a genetic variant shown to be under the control of one genetic locus (the Mup-alocus), differed by a single peptide. Components 1 and 3 had a number of peptides in common plus several peptides unique to each. The peptide map of any given component did not differ between sexes or between the strains investigated.