| Autor: |
van Hofsten, P, Faye, I, Kockum, K, Lee, J Y, Xanthopoulos, K G, Boman, I A, Boman, H G, Engström, A, Andreu, D, Merrifield, R B |
| Zdroj: |
Proceedings of the National Academy of Sciences of the United States of America; April 1985, Vol. 82 Issue: 8 p2240-2243, 4p |
| Abstrakt: |
Two cDNA clones containing coding information for cecropin B from the Cecropia moth (Hyalophora cecropia) were identified by means of a synthetic probe. Sequencing of the two inserts showed that cecropin B is processed from a 62-amino acid residue precursor molecule including a 26-residue leader peptide and a COOH-terminal glycine residue. The latter presumably donates the nitrogen of the amide group present on the COOH-terminal leucine residue of the mature cecropin B. The sequence deduced for the mature cecropin B differed in the COOH-terminal region from the tentative structure previously determined by carboxypeptidase digestion. To settle the discrepancy, cecropin B was synthesized according to the cDNA sequence with an amidated COOH-terminal leucine. Natural and synthetic cecropin B were found to be indistinguishable with respect to electrophoretic mobility and antibacterial activity against seven different bacteria. The COOH-terminal tetrapeptides were isolated from both natural and synthetic cecropin B and found to be indistinguishable. The correct sequence for cecropin B is (formula; see text). |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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