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. 1986 May;83(10):3223–3227. doi: 10.1073/pnas.83.10.3223

Cloning, sequence, and expression of bovine interleukin 2.

D P Cerretti, K McKereghan, A Larsen, M A Cantrell, D Anderson, S Gillis, D Cosman, P E Baker
PMCID: PMC323485  PMID: 3517854

Abstract

Interleukin 2 (IL-2) cDNA clones have been isolated from both human and murine sources. We report here the isolation of a cDNA clone encoding bovine IL-2. This was accomplished by screening a cDNA library constructed from lectin-stimulated bovine lymph node cells, using a human IL-2 probe. Bovine IL-2 is composed of 155 amino acids and has a predicted molecular weight of 19,555. Alignment of the amino acid sequence with human IL-2 indicates that mature bovine IL-2 is composed of 135 amino acids and has a predicted molecular weight of 15,452. It has an amino acid homology of 65% with human IL-2 and 50% with murine IL-2. Bovine IL-2 is unique among IL-2 homologs in that it has a single N-linked glycosylation site. Biologically active bovine IL-2 was synthesized in an Escherichia coli expression system.

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Selected References

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