A major urinary protein of the male rat was purified by a combination of (NH4)2SO4 fractionation and chromatography on DEAE-cellulose. The molecular weight, sedimentation coefficient (s020,w) and isoelectric point were determined to be 26 400, 2.2.S and pH 3.4, respectively. Hexose, glucosamine and sialic acid were shown tobe 2%, 1.6% and 1.4%. The amino acid composition was also established. The electrophoretic migration was studied in starch-gel and immunoelectrophoretic systems. In the immunoelectrophoretic system, the purified protein migrated similarly to one of the major components of the total urinary proteins previously designated as a α2-globulin.
ASJC Scopus subject areas
- Molecular Biology