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Digestive proteinases of yellow mealworm (Tenebrio molitor) larvae: purification and characterization of a trypsin-like proteinase.
Biochemistry (Mosc). 2005 Mar; 70(3):300-5.B

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 pI 7.4. The enzyme was also characterized by temperature optimum at 55 degrees C, pH optimum at 8.5, and K(m) 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.

Authors+Show Affiliations

Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow 119071, Russia.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

Language

eng

PubMed ID

15823084

Citation

Tsybina, T A., et al. "Digestive Proteinases of Yellow Mealworm (Tenebrio Molitor) Larvae: Purification and Characterization of a Trypsin-like Proteinase." Biochemistry. Biokhimiia, vol. 70, no. 3, 2005, pp. 300-5.
Tsybina TA, Dunaevsky YE, Belozersky MA, et al. Digestive proteinases of yellow mealworm (Tenebrio molitor) larvae: purification and characterization of a trypsin-like proteinase. Biochemistry (Mosc). 2005;70(3):300-5.
Tsybina, T. A., Dunaevsky, Y. E., Belozersky, M. A., Zhuzhikov, D. P., Oppert, B., & Elpidina, E. N. (2005). Digestive proteinases of yellow mealworm (Tenebrio molitor) larvae: purification and characterization of a trypsin-like proteinase. Biochemistry. Biokhimiia, 70(3), 300-5.
Tsybina TA, et al. Digestive Proteinases of Yellow Mealworm (Tenebrio Molitor) Larvae: Purification and Characterization of a Trypsin-like Proteinase. Biochemistry (Mosc). 2005;70(3):300-5. PubMed PMID: 15823084.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Digestive proteinases of yellow mealworm (Tenebrio molitor) larvae: purification and characterization of a trypsin-like proteinase. AU - Tsybina,T A, AU - Dunaevsky,Y E, AU - Belozersky,M A, AU - Zhuzhikov,D P, AU - Oppert,B, AU - Elpidina,E N, PY - 2005/4/13/pubmed PY - 2005/9/2/medline PY - 2005/4/13/entrez SP - 300 EP - 5 JF - Biochemistry. Biokhimiia JO - Biochemistry (Mosc) VL - 70 IS - 3 N2 - 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 pI 7.4. The enzyme was also characterized by temperature optimum at 55 degrees C, pH optimum at 8.5, and K(m) 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. SN - 0006-2979 UR - https://www.unboundmedicine.com/medline/citation/15823084/Digestive_proteinases_of_yellow_mealworm__Tenebrio_molitor__larvae:_purification_and_characterization_of_a_trypsin_like_proteinase_ L2 - http://protein.bio.msu.ru/biokhimiya/contents/v70/full/70030370.html DB - PRIME DP - Unbound Medicine ER -