Abstract
An hepatically synthesized sex-dependent protein ( α 2u), isolated from male rat urine, has been compared with other similarly designated rat proteins. Using a specific antiserum prepared against α 2u, immunological analysis revealed no cross reaction with a sex-dependent protein prepared from unsonicated rat liver homogenates. An α-globulin separated from urine by molecular sieving and chromatography on CM-cellulose was shown to be immunologically identical with α 2u. This α-globulin exhibited only a single electrophoretic band (acrylamide gel) whereas α 2u contained multiple species of protein having different isoelectric points. The single isoelectric form obtained from CM-cellulose migrated electrophoretically as did the major α 2u (5.2) component. Further studies showed that CM-cellulose could be used to separate the various isoelectric species of α 2u. Antisera to murine, urinary sex-dependent proteins have been shown to cross react with some urinary proteins in the rat. However, an antiserum to α 2u did not cross react with any murine urinary proteins.
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