Premium
Two‐dimensional electrophoresis of proteins from different lobes of the rat prostate and seminal vesicle
Author(s) -
Gerhardt P.,
Mevåg B.,
Rui H.,
Purvis K.,
Tveter K. J.
Publication year - 1985
Publication title -
the prostate
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.295
H-Index - 123
eISSN - 1097-0045
pISSN - 0270-4137
DOI - 10.1002/pros.2990070309
Subject(s) - secretion , secretory protein , biology , seminal vesicle , secretory vesicle , molecular mass , lobe , prostate , vesicle , gel electrophoresis , microbiology and biotechnology , biochemistry , endocrinology , medicine , chemistry , anatomy , enzyme , exocytosis , genetics , cancer , membrane
Two‐dimensional ISO‐DALT electrophoresis of cytosols and secretions from various lobes of the rat prostate gland and seminal vesicle reveals major differences in intracellular and secretory protein patterns. This study confirms a previous study utilizing one‐dimensional electrophoresis. The dorsal lobe and coagulating gland appear to secrete predominantly relatively basic proteins (molecular mass, MM, 70,000–200,000 daltons, pI > 7) in contrast to the ventral lobe, which secretes proteins of a more acidic character (pI 4–5). The majority of proteins in the latter case appear to represent subunits of the major secretory protein of the rat ventral prostate, prostatein. At least one secretory protein is relatively specific for the lateral lobe (MM 16,000 daltons, pI 4.5). The vesicular secretion also contains relatively greater quantities of basic proteins than acidic but with varying molecular mass (12,000–100,000 daltons). This study extends the search for specific protein markers for different lobes of the rat accessory sex glands and provides additional biochemical data which can be exploited in the future to isolate selected secretory proteins on a large scale for antibody production.