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Digestive proteinases of yellow mealworm (Tenebrio molitor) larvae: Purification and characterization of a trypsin-like proteinase
| Content Provider | Semantic Scholar |
|---|---|
| Author | Tsybina, T. A. Dunaevsky, Yakov E. Belozersky, Mikhail A. Zhuzhikov, Dmitry P. Oppert, Brenda Elpidina, Elena N. |
| Copyright Year | 2005 |
| Abstract | A new trypsin-like proteinase was purified to homogeneity from the posterior midgut of Tenebrio molitor larvae by ion-exchange chromatography on DEAE-Sephadex A-50 and gel filtration on Superdex-75. The isolated enzyme had molecular mass of 25.5 kD and pI7.4. The enzyme was also characterized by temperature optimum at 55°C, pH optimum at 8.5, and Km value of 0.04 mM (for hydrolysis of Bz-Arg-pNA). According to inhibitor analysis the enzyme is a trypsin-like serine proteinase stable within the pH range of 5.0–9.5. The enzyme hydrolyzes peptide bonds formed by Arg or Lys residues in the P1 position with a preference for relatively long peptide substrates. The N- terminal amino acid sequence, IVGGSSISISSVPXQIXLQY, shares 50–72% identity with other insect trypsin-like proteinases, and 44–50% identity to mammalian trypsins. The isolated enzyme is sensitive to inhibition by plant proteinase inhibitors and it can serve as a suitable target for control of digestion in this stored product pest. |
| Starting Page | 300 |
| Ending Page | 305 |
| Page Count | 6 |
| File Format | PDF HTM / HTML |
| DOI | 10.1007/s10541-005-0115-2 |
| Alternate Webpage(s) | https://naldc.nal.usda.gov/download/13475/PDF |
| Alternate Webpage(s) | http://protein.bio.msu.ru/biokhimiya/contents/v70/pdf/bcm_0300.pdf |
| PubMed reference number | 15823084 |
| Alternate Webpage(s) | https://doi.org/10.1007/s10541-005-0115-2 |
| Journal | Medline |
| Volume Number | 70 |
| Journal | Biochemistry (Moscow) |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
