| Autor: |
Verkuylen AJ; CSIRO Division of Biomolecular Engineering, Parkville, Victoria, Australia., Frenkel MJ, Savin KW, Dopheide TA, Ward CW |
| Jazyk: |
angličtina |
| Zdroj: |
Molecular and biochemical parasitology [Mol Biochem Parasitol] 1993 Apr; Vol. 58 (2), pp. 325-32. |
| DOI: |
10.1016/0166-6851(93)90055-3 |
| Abstrakt: |
A glycoprotein, with apparent molecular weight in SDS-polyacrylamide gels of 37 kDa, has been isolated from the excretory-secretory (ES) products of the adult stage of Trichostrongylus colubriformis, a parasitic nematode. This protein is the major ES product recognized in immunoblots by lymph from a naturally infected sheep. A synthetic oligonucleotide, based on peptide sequence data from a digest of the purified protein was used to successfully screen a cDNA library. A cDNA clone was isolated which encoded a presumptive protein precursor of 220 amino acids that contained a 63 amino acid region of which more than 35% of the residues were proline, three peptide sequences determined from the natural component, and three potential N-glycosylation sites, consistent with the protein being isolated from the lectin-bound fraction of the adult ES products. The presumptive, processed, amino terminus encoded by the cDNA clone was preceded by a signal-like, hydrophobic-rich region of 16 amino acids. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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