Abstract
The structural gene for diphtheria toxin, tox, has been modified at its Sph I site by the introduction of an oligonucleotide linker encoding a unique Pst I restriction endonuclease site and a synthetic oligonucleotide encoding α-melanocyte-stimulating hormone (α-MSH). The resulting fusion gene directs the expression of a diphtheria toxin-related α-MSH hybrid protein in which the diphtheria toxin receptor-binding domain has been replaced with α-MSH sequences. The chimeric toxin has been partially purified from periplasmic extracts of recombinant Escherichia coli K-12 and has been found to be selectively toxic for α-MSH receptor-positive human malignant melanoma NEL-M1 cells in vitro.
Original language | English (US) |
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Pages (from-to) | 8258-8262 |
Number of pages | 5 |
Journal | Proceedings of the National Academy of Sciences of the United States of America |
Volume | 83 |
Issue number | 21 |
DOIs | |
State | Published - 1986 |
Externally published | Yes |
ASJC Scopus subject areas
- General