Peptidase inhibitors from the salivary glands of the cockroach Nauphoeta cinerea
| Autor: | Barbara Kludkiewicz, Yuliya Taranushenko, František Sehnal, Konstantin Vinokurov, Dalibor Kodrík |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Signal peptide
Molecular Sequence Data Cockroaches Peptide Biochemistry medicine Animals Protease Inhibitors Amino Acid Sequence Molecular Biology chemistry.chemical_classification Chymotrypsin Base Sequence biology Subtilisin Trypsin biology.organism_classification Proteinase K Molecular biology Blaberidae Amino acid Gene Expression Regulation chemistry Insect Science biology.protein Peptide Hydrolases medicine.drug |
| Zdroj: | Insect Biochemistry and Molecular Biology. 39:920-930 |
| ISSN: | 0965-1748 |
| DOI: | 10.1016/j.ibmb.2009.11.002 |
| Popis: | Inhibitory activity against subtilisin, proteinase K, chymotrypsin and trypsin was detected in the salivary glands and saliva of the cockroach Nauphoeta cinerea (Blattoptera: Blaberidae). Fractionation of the salivary glands extract by affinity chromatography followed by reverse-phase HPLC yielded five subtilisin-inhibiting peptides with molecular masses ranging from 5 to 14 kDa. N-terminal sequences and subsequently full-length cDNAs of inhibitors designated NcPIa and NcPIb were obtained. The NcPIa cDNA contains 216 nucleotides and encodes a pre-peptide of 72 amino-acid residues of which 19 make up the signal peptide. The cDNA of NcPIb consists of 240 nucleotides and yields a putative secretory peptide of 80 amino-acid residues. Mature NcPIa (5906.6 Da, 53 residues) and NcPIb (6713.3 Da, 60 residues) are structurally similar (65.4% amino acid overlap) single-domain Kazal-type peptidase inhibitors. NcPIa with Arg in P1 position and typical Kazal motif VCGSD interacted stoichiometrically (1:1) with subtilisin and was slightly less active against proteinase K. NcPIb with Leu in P1 and modified Kazal motif ICGSD had similar activity on subtilisin and no on proteinase K but was active on chymotrypsin. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect