Abstract
The effect of neuraminidase on glycoproteins with endstanding N-acetylneuraminyl groups results in a significant decrease of their electrophoretic mobilities. This phenomenon was used for the identification of glycoproteins present in the human seminal plasma. Immunoelectrophoretic analyses before and after treatment with neuraminidase revealed that several protein constituents including various enzymes are glycoproteins with terminal N-acetylneuraminyl groups, most of which are secreted by the prostate gland. Not all types of glycoproteins can be detected by the methods employed. There is reason to believe that some of the glycoproteins originating in the seminal vesicles do not react with precipitating antisera specifically directed against human seminal plasma proteins.
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