Abstract
Analysis of chemically cross-linked recombinant human tumor necrosis factor (rTNF) on sodium dodecyl sulfate polyacrylamide gel electrophoresis revealed the presence of three distinct molecular forms which correspond to trimers, dimers, and monomers. The cross-linking procedure appeared to enhance the antigenicity of these molecular forms of rTNF as determined by Western blot analysis. Cross-linking was unaffected by 2% Nonidet P-40, high concentrations of human serum albumin, or 60% normal human serum. Sodium dodecyl sulfate (0.08%) completely abolished the cross-linking of rTNF. This paper demonstrates that rTNF, at a concentration as low as 0.8 ng/ml, exists solely in the trimeric form in solution under nondenaturing conditions.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 267-275 |
| Number of pages | 9 |
| Journal | Journal of Biological Response Modifiers |
| Volume | 7 |
| Issue number | 3 |
| State | Published - 1988 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Cancer Research
- Immunology
- Pharmacology
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Analysis of the molecular organization of recombinant human tumor necrosis factor (rTNF) in solution using ethylene glycolbis (succinimidylsuccinate) as the cross-linking reagent. / Lam, Kit; Scuderi, P.; Salmon, S. E.
In: Journal of Biological Response Modifiers, Vol. 7, No. 3, 1988, p. 267-275.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Analysis of the molecular organization of recombinant human tumor necrosis factor (rTNF) in solution using ethylene glycolbis (succinimidylsuccinate) as the cross-linking reagent
AU - Lam, Kit
AU - Scuderi, P.
AU - Salmon, S. E.
PY - 1988
Y1 - 1988
N2 - Analysis of chemically cross-linked recombinant human tumor necrosis factor (rTNF) on sodium dodecyl sulfate polyacrylamide gel electrophoresis revealed the presence of three distinct molecular forms which correspond to trimers, dimers, and monomers. The cross-linking procedure appeared to enhance the antigenicity of these molecular forms of rTNF as determined by Western blot analysis. Cross-linking was unaffected by 2% Nonidet P-40, high concentrations of human serum albumin, or 60% normal human serum. Sodium dodecyl sulfate (0.08%) completely abolished the cross-linking of rTNF. This paper demonstrates that rTNF, at a concentration as low as 0.8 ng/ml, exists solely in the trimeric form in solution under nondenaturing conditions.
AB - Analysis of chemically cross-linked recombinant human tumor necrosis factor (rTNF) on sodium dodecyl sulfate polyacrylamide gel electrophoresis revealed the presence of three distinct molecular forms which correspond to trimers, dimers, and monomers. The cross-linking procedure appeared to enhance the antigenicity of these molecular forms of rTNF as determined by Western blot analysis. Cross-linking was unaffected by 2% Nonidet P-40, high concentrations of human serum albumin, or 60% normal human serum. Sodium dodecyl sulfate (0.08%) completely abolished the cross-linking of rTNF. This paper demonstrates that rTNF, at a concentration as low as 0.8 ng/ml, exists solely in the trimeric form in solution under nondenaturing conditions.
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UR - http://www.scopus.com/inward/citedby.url?scp=0023923940&partnerID=8YFLogxK
M3 - Article
C2 - 3392553
AN - SCOPUS:0023923940
VL - 7
SP - 267
EP - 275
JO - Journal of Immunotherapy
JF - Journal of Immunotherapy
SN - 1524-9557
IS - 3
ER -