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Diversity of digestive proteinases in Tenebrio molitor (Coleoptera: Tenebrionidae) larvae.
Comp Biochem Physiol B Biochem Mol Biol. 2006 Oct; 145(2):126-37.CB

Abstract

The spectrum of Tenebrio molitor larval digestive proteinases was studied in the context of the spatial organization of protein digestion in the midgut. The pH of midgut contents increased from 5.2-5.6 to 7.8-8.2 from the anterior to the posterior. This pH gradient was reflected in the pH optima of the total proteolytic activity, 5.2 in the anterior and 9.0 in the posterior midgut. When measured at the pH and reducing conditions characteristic of each midgut section, 64% of the total proteolytic activity was in the anterior and 36% in the posterior midgut. In the anterior midgut, two-thirds of the total activity was due to cysteine proteinases, whereas the rest was from serine proteinases. In contrast, most (76%) of the proteolytic activity in the posterior midgut was from serine proteinases. Cysteine proteinases from the anterior were represented by a group of anionic fractions with similar electrophoretic mobility. Trypsin-like activity was predominant in the posterior midgut and was due to one cationic and three anionic proteinases. Chymotrypsin-like proteinases also were prominent in the posterior midgut and consisted of one cationic and four anionic proteinases, four with an extended binding site. Latent proteinase activity was detected in each midgut section. These data support a complex system of protein digestion, and the correlation of proteinase activity and pH indicates a physiological mechanism of enzyme regulation in the gut.

Authors+Show Affiliations

Department of Entomology, Biological Faculty, Moscow State University, Moscow 119992, Russia.No affiliation info availableNo 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

16859942

Citation

Vinokurov, K S., et al. "Diversity of Digestive Proteinases in Tenebrio Molitor (Coleoptera: Tenebrionidae) Larvae." Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology, vol. 145, no. 2, 2006, pp. 126-37.
Vinokurov KS, Elpidina EN, Oppert B, et al. Diversity of digestive proteinases in Tenebrio molitor (Coleoptera: Tenebrionidae) larvae. Comp Biochem Physiol B Biochem Mol Biol. 2006;145(2):126-37.
Vinokurov, K. S., Elpidina, E. N., Oppert, B., Prabhakar, S., Zhuzhikov, D. P., Dunaevsky, Y. E., & Belozersky, M. A. (2006). Diversity of digestive proteinases in Tenebrio molitor (Coleoptera: Tenebrionidae) larvae. Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology, 145(2), 126-37.
Vinokurov KS, et al. Diversity of Digestive Proteinases in Tenebrio Molitor (Coleoptera: Tenebrionidae) Larvae. Comp Biochem Physiol B Biochem Mol Biol. 2006;145(2):126-37. PubMed PMID: 16859942.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Diversity of digestive proteinases in Tenebrio molitor (Coleoptera: Tenebrionidae) larvae. AU - Vinokurov,K S, AU - Elpidina,E N, AU - Oppert,B, AU - Prabhakar,S, AU - Zhuzhikov,D P, AU - Dunaevsky,Y E, AU - Belozersky,M A, Y1 - 2006/05/23/ PY - 2005/12/22/received PY - 2006/05/15/revised PY - 2006/05/16/accepted PY - 2006/7/25/pubmed PY - 2007/7/26/medline PY - 2006/7/25/entrez SP - 126 EP - 37 JF - Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology JO - Comp Biochem Physiol B Biochem Mol Biol VL - 145 IS - 2 N2 - The spectrum of Tenebrio molitor larval digestive proteinases was studied in the context of the spatial organization of protein digestion in the midgut. The pH of midgut contents increased from 5.2-5.6 to 7.8-8.2 from the anterior to the posterior. This pH gradient was reflected in the pH optima of the total proteolytic activity, 5.2 in the anterior and 9.0 in the posterior midgut. When measured at the pH and reducing conditions characteristic of each midgut section, 64% of the total proteolytic activity was in the anterior and 36% in the posterior midgut. In the anterior midgut, two-thirds of the total activity was due to cysteine proteinases, whereas the rest was from serine proteinases. In contrast, most (76%) of the proteolytic activity in the posterior midgut was from serine proteinases. Cysteine proteinases from the anterior were represented by a group of anionic fractions with similar electrophoretic mobility. Trypsin-like activity was predominant in the posterior midgut and was due to one cationic and three anionic proteinases. Chymotrypsin-like proteinases also were prominent in the posterior midgut and consisted of one cationic and four anionic proteinases, four with an extended binding site. Latent proteinase activity was detected in each midgut section. These data support a complex system of protein digestion, and the correlation of proteinase activity and pH indicates a physiological mechanism of enzyme regulation in the gut. SN - 1096-4959 UR - https://www.unboundmedicine.com/medline/citation/16859942/Diversity_of_digestive_proteinases_in_Tenebrio_molitor__Coleoptera:_Tenebrionidae__larvae_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S1096-4959(06)00133-3 DB - PRIME DP - Unbound Medicine ER -