Heterogeneity of rat TCGF defined by Mono P isoelectric focusing.
Interleukin-2 (IL-2) prepared from Con A-activated rat spleen cells was partially purified using hydroxylapatite chromatography (HTP) and chromatofocusing on Mono P. IL-2 eluted in a major peak between 0.1 and 0.25 M NaCl in PBS (purification factor 36-fold) and in a second peak in the high salt elution (purification factor 5-fold). When analysed on Mono P, the major peak was found to resolve into four components with apparent pI values in the range of 7.05-5.80; further activity eluted in the high salt fraction. Similar patterns were observed using high salt eluted activity with minor variations in the apparent pI values. Neuraminidase treatment caused a shift in IL-2 charge towards more basic pI values. This analysis of the multiple species of IL-2 suggests that part of the heterogeneity may be due to variation in the degree of sialylation of the peptide chain.
D000818:Animals; D007376:Interleukin-2 / Q000302:isolation & purification*; D007525:Isoelectric Focusing; D009439:Neuraminidase; D051381:Rats; D011919:Rats, Inbred Strains
D007376:Interleukin-2; D009439:Neuraminidase