PURIFICATION OF A SULFATED SECRETORY PROTEIN FROM THE ADENOHYPOPHYSIS - IMMUNOCHEMICAL EVIDENCE THAT SIMILAR MACROMOLECULES ARE PRESENT IN OTHER GLANDS

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  • 1 January 1983
    • journal article
    • research article
    • Vol. 31  (1) , 94-98
    • PMID:6413211
Abstract
A sulfated secretory protein (apparent MW .apprx. 70,000; isoelectric point .apprx. 4.8) recently identified as a minor component of mammotroph granules was purified by ion-exchange chromatography on DEAE-Sephadex followed by preparative slab gel electrophoresis from homogenates of bovine anterior pituitary glands pulse-labeled with [35S] sulfate. The homogeneity of the final product was established by 1-dimensional as well as by 2-dimensional gel electrophoresis followed by fluorography to reveal labeled polypeptides. Specific antibodies were generated against the purified protein. Immunodiffusion and radioimmunolabeling of polyacrylamide gels revealed that proteins immunologically related to the adenohypophyseal sulfated component exist in other glands, such as the neurointermediate pituitary and adrenal medulla. The adenohypophyseal sulfated component might belong to a family of proteins which might play a widespread, though not general role in the secretory process.