Purification and characterization of two forms of rat interleukin-2.

Abstract:

:Rat IL-2 produced by spleen cells in culture with concanavalin A was purified using gel filtration, hydrophobic chromatography, and ion-exchange chromatography. At least two forms of rat IL-2 were found to be separable by ion-exchange chromatography. These two forms have been designated form I and form II. Form I of rat IL-2 was purified by a factor of 1297 and found to have a pI of 6.4. Form II was purified by a factor of 669 and found to have a pI between 5.4 and 6.1. Lectin chromatography was used to demonstrate that these two forms most likely differ in the extent of glycosylation. In the presence of tunicamycin the production of form II was significantly reduced. The two forms of rat IL-2 differ in their abilities to promote a mixed-lymphocyte reaction. Their differences in glycosylation may be the reason for these differences in activity.

journal_name

Cell Immunol

journal_title

Cellular immunology

authors

Thompson LP,Di Sabato G

doi

10.1016/0008-8749(88)90251-1

subject

Has Abstract

pub_date

1988-06-01 00:00:00

pages

12-26

issue

1

eissn

0008-8749

issn

1090-2163

pii

0008-8749(88)90251-1

journal_volume

114

pub_type

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