1986
DOI: 10.1016/0022-1759(86)90529-6
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Simple preparative two-step purification of interleukin-2 from culture medium of lectin stimulated normal human lymphocytes

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Cited by 7 publications
(3 citation statements)
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“…Natural human IL‐2 (hIL‐2) is a hydrophobic 15.5 kDa globular glycosylated protein with a various degree of glycosylation, as estimated from gel filtration. It is glycosylated at position 3 by the amino acid thrieonine 47. Its primary structure is represented by 133 amino acids, which shows no significant homologies in the primary structure with other cytokines 48, 49.…”
Section: Physical Properties and Structurementioning
confidence: 99%
“…Natural human IL‐2 (hIL‐2) is a hydrophobic 15.5 kDa globular glycosylated protein with a various degree of glycosylation, as estimated from gel filtration. It is glycosylated at position 3 by the amino acid thrieonine 47. Its primary structure is represented by 133 amino acids, which shows no significant homologies in the primary structure with other cytokines 48, 49.…”
Section: Physical Properties and Structurementioning
confidence: 99%
“…The IL-2-dependent proliferation was determined by incubation of MNC in the presence of 10 U/ml leetin-free IL-2 with or without addition of 1 ;Mg/ml eoncanavalin A (Con A) (Sifin) for 72 h. One microcurie of [-'H]thymidine was added to each well 12-18 h before harvesting. Lectin-free IL-2 was prepared as described in detail elsewhere [5]. In brief, MNC were stimulated with Con A and phorbol myristate acetate (PMA) in serum-free Iscove's medium for 6 h. After washing, the cells were cultured for a further 2 days without Con A.…”
Section: Methodsmentioning
confidence: 99%
“…The cell-free supernatant was tested for IL-2 activity on a mouse CTL line. One unit of IL-2 per ml was defined as the IL-2 concentration which gives half the maximum proliferation in the standard assay [5].…”
Section: Methodsmentioning
confidence: 99%