PMID: 6979358Jul 1, 1982Paper

Purification of colony-stimulating factor by affinity chromatography.

Blood
A Waheed, R K Shadduck

Abstract

Studies were undertaken to determine whether L-cell-derived colony-stimulating factor (CSF) could be purified by a single step affinity chromatographic technique. A quantity of 100 X 10(6) units of purified anti-CSF was coupled to cyanogen bromide activated Sepharose 4B; colony assays revealed complete binding of the antibodies to the gel. Three 10-liter pools of serum-free L-cell CSF were concentrated by ultrafiltration, applied to the gel, and eluted with a low pH, high molarity buffer. Recovery of CSF ranged from 68%-100% with greater than 1000-fold decreases in protein content. Specific activity of the purified CSF ranged from 2.8 to 5.9 X 10(7) U of CSF/mg protein. Following iodination, each purified pool of CSF revealed a major 63,000-dalton peak of radioactivity that comigrated with CSF activity in SDS-acrylamide gels. In addition, several smaller peaks of 50,000 and 40,000 molecular weight were also detected. Approximately two-thirds of the purified CSF was adherent to concanavalin-A with elution by a competing sugar. Electrophoretic mobility was retarded by incubation with neuraminidase. These chromatographic studies confirm the observation that CSF is a glycoprotein but also suggest variable degrees of glycosylation o...Continue Reading

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