Abstract
Antibacterial activity was induced in the hemolymph of larvae of the coleopteran Tenebrio molitor by injection of Escherichia coli* An antibacterial protein, named tenecin 1, was purified to homogeneity from the larval hemolymph and characterized. A cDNA clone for tenecin 1 was isolated and its complete sequence was determined. This protein was found to inhibit the growth of Gram-positive bacteria and to consist of 43-amino acid residues including six cysteine residues. The disulfide structure of tenecin 1 was determined by sequencing cysteine containing peptides obtained by digesting tenecin 1 with endopep-tidase Lys-C, trypsin, and thermolysin. The amino acid sequence and its disulfide bonds were similar to those of sapecin and sapecin C, antibacterial proteins of Sarcophaga peregrina.
Original language | English |
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Pages (from-to) | 53-58 |
Number of pages | 6 |
Journal | Journal of biochemistry |
Volume | 116 |
Issue number | 1 |
DOIs | |
Publication status | Published - 1994 Jul |
Externally published | Yes |
Keywords
- Antibacterial protein
- Coleopteran insect
- Inducible protein
- Molecular cloning
- Purification
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology