Physicochemical characterization of cytostatic factors released from human monocytes
- 1 October 1982
- journal article
- research article
- Published by American Society for Microbiology in Infection and Immunity
- Vol. 38 (1), 67-73
- https://doi.org/10.1128/iai.38.1.67-73.1982
Abstract
Cultured human monocytes released cytostatic activity upon in vitro activation with lymphokines and lipopolysaccharide. This activity was mainly due to the presence of 2 different cytostatic factors, termed CstF I and II, which were separated by ion-exchange chromatography. At neutral pH, CstF I bound to the weak anion exchanger DEAE-Sephacel but not to the weak cation exchanger CM-Sepharose; CstF II bound to CM-Sepharose but not to DEAE-Sephacel. The MW of CstF I and II as determined by gel filtration were 55,000 and 40,000, respectively. Upon chromatofocusing, CstF I behaved as if it had an isoelectric point of 5.3. Neither CstF I nor CstF II bound specifically to concanavalin A-Sepharose, indicating the absence of carbohydrate residues containing .alpha.-D-mannopyranosyl, .alpha.-D-glucopyranosyl or sterically related components. Both factors were susceptible to inactivation by proteinase K, demonstrating their protein nature. CstF II was purified more than 3000-fold upon chromatography on CM-Sepharose and Sephacryl S-200. Ion-exchange chromatography and chromatofocusing of CstF I removed 97% of the proteins in the monocyte supernatant, but only 15% of the activity was recovered, resulting in a 5-fold purification of CstF I.This publication has 26 references indexed in Scilit:
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