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Soluble Proteins of Guinea Pig Seminal Vesicle Lumen: Purification and Partial Characterization

Luminal contents of guinea pig seminal vesicle were extracted with 0.154 M NaCl and the soluble protein fraction was studied by DEAE‐cellulose and Sephadex G‐100 column chromatography; anionic, cationic, and SDS‐polyacrylamide disc gel electrophoresis; isoelectric focusing; molecular weight determinations by SDS‐polyacrylamide disc gel electrophoresis; analysis for neutral carbohydrate; sucrose density‐gradient centrifugation for determination of sedimentation coefficients; and amino acid analyses. Four protein fractions (referred to as proteins 1, 2, 3, and 4 in order of elution) were obtained by DEAE‐cellulose column chromatography. Proteins 1, 2, and 4 gave single major bands in multiple disc gel electrophoretic systems. Protein 3 gave one major band and one minor component believed to be a fragment of a primary vesicular protein.