Abstract
A method for the preparation and purification of large amounts (grams) of a conjugate containing recombinant CD4 antigen (rCD4) and chemically deglycosylated ricin A chain (dgA) is described. The cross-linking of rCD4 and dgA molecules was accomplished with N-succinimidyl-oxycarbonyl-α-methyl-(2-pyridyldithio)toluene (SMPT). The rCD4-dgA conjugate was purified by an automatic liquid chromatography system consisting of Blue Sepharose CL-4B and Sephacryl S-200HR Pharmacia Bioprocess columns. The purified, endotoxin-free rCD4-dgA conjugate had a stable (hindered) disulfide bond between rCD4 and dgA and was able to efficiently kill a human T cell line infected HIV-1.
Original language | English (US) |
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Pages (from-to) | 135-141 |
Number of pages | 7 |
Journal | Journal of Immunological Methods |
Volume | 126 |
Issue number | 1 |
DOIs | |
State | Published - Jan 24 1990 |
Keywords
- CD4
- Human immunodeficiency virus
- Immunoconjugate
- Ricin A chain
ASJC Scopus subject areas
- Immunology and Allergy
- Immunology