Abstract
CSF-1 was isolated from a large volume of human normal urine (10,000 l), using the following 5 stages of purification: concentration by dialysis, silica gel adsorption, hydrophobic chromatography on phenyl-Sepharose CL-6B, fast protein liquid chromatography (FPLC) and finally preparative electrophoresis on polyacrylamide gels. We have isolated 8 mg of purified CSF-1 which migrated as a single band under non-reducing conditions in SDS-PAGE (staining with Coomassie Blue and the sensitive silver techniques). But in the presence of dithiothreitol, the SDS-PAGE pattern revealed a minor second band with a molecular mass of 50,000 Da. CSF-1 was purified 100,000-fold and has a specific activity of 2.16 X 10(7) units/mg protein. Its apparent molecular mass is 57,000 Da with an isoelectric point, pI = 5.8-6.0. The amino-acid composition is reported and compared with that of murine CSF-1. The carbohydrate content (sialic acid, sulphate groups, N-acetylglucosamine, N-acetylgalactosamine) was also determined, and it shows that CSF is a glycoprotein.
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