Autor: |
Samy, T S, Hahm, K S, Modest, E J, Lampman, G W, Keutmann, H T, Umezawa, H, Herlihy, W C, Gibson, B W, Carr, S A, Biemann, K |
Zdroj: |
Journal of Biological Chemistry; January 1983, Vol. 258 Issue: 1 p183-191, 9p |
Abstrakt: |
The antitumor protein macromomycin is a single chain polypeptide of 112 amino acid residues cross-linked by two intramolecular disulfide bonds. The protein was reduced and S-alkylated with 2-mercaptoethanol in 8 M urea followed by treatment with iodoacetic acid. Tryptic digestion of tetra-S-carboxymethyl macromomycin gave four tryptic peptides which were fractionated by gel permeation on Sephadex G-50. The amino acid sequence of the tryptic peptides and the overlap sequences were determined by a combination of automated Edman degradation analysis, gas chromatographic mass spectrometry, and fast atom bombardment mass spectrometry. A comparison of the structures of macromomycin, actinoxanthin, and neocarzinostatin suggests that they belong to a family of related proteins. |
Databáze: |
Supplemental Index |
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