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Protease activity in gut of Daphnia magna: evidence for trypsin and chymotrypsin enzymes.
Comp Biochem Physiol B Biochem Mol Biol. 2004 Mar; 137(3):287-96.CB

Abstract

Two major protease activities were present in gut homogenates of the cladoceran crustacean Daphnia magna: (i) a trypsin activity that hydrolysed the synthetic substrate N-benzoyl-dl-arginine p-nitroanilide and was strongly inhibited by N-p-tosyl-lysine chloroketone (TLCK) and 4-(amidinophenyl)methanesulfonyl fluoride (APMSF) and not inhibited by chymostatin; and (ii) a chymotrypsin activity that hydrolysed synthetic chymotrypsin substrates containing more than one amino acid, did not hydrolyse N-benzoyl-l-tyrosine p-nitroanilide, and was strongly inhibited by chymostatin and not by TLCK and APMSF. Both activities had alkaline pH optima (pH 7-10), but were shown to be due to distinct types of proteases. These two enzyme activities accounted for 75-83% of the proteolytic activity of gut contents. Substrate SDS-polyacrylamide gel electrophoresis revealed nine different proteases ranging from 15 to 73 kDa.

Authors+Show Affiliations

Limnological Institute, University of Constance, 78434 Konstanz, Germany. eric.vonelert@uni-konstanz.deNo 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

Language

eng

PubMed ID

15050516

Citation

von Elert, Eric, et al. "Protease Activity in Gut of Daphnia Magna: Evidence for Trypsin and Chymotrypsin Enzymes." Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology, vol. 137, no. 3, 2004, pp. 287-96.
von Elert E, Agrawal MK, Gebauer C, et al. Protease activity in gut of Daphnia magna: evidence for trypsin and chymotrypsin enzymes. Comp Biochem Physiol B Biochem Mol Biol. 2004;137(3):287-96.
von Elert, E., Agrawal, M. K., Gebauer, C., Jaensch, H., Bauer, U., & Zitt, A. (2004). Protease activity in gut of Daphnia magna: evidence for trypsin and chymotrypsin enzymes. Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology, 137(3), 287-96.
von Elert E, et al. Protease Activity in Gut of Daphnia Magna: Evidence for Trypsin and Chymotrypsin Enzymes. Comp Biochem Physiol B Biochem Mol Biol. 2004;137(3):287-96. PubMed PMID: 15050516.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Protease activity in gut of Daphnia magna: evidence for trypsin and chymotrypsin enzymes. AU - von Elert,Eric, AU - Agrawal,Manish Kumar, AU - Gebauer,Christine, AU - Jaensch,Heike, AU - Bauer,Ulrike, AU - Zitt,Anja, PY - 2003/05/28/received PY - 2003/11/20/revised PY - 2003/11/21/accepted PY - 2004/3/31/pubmed PY - 2005/4/9/medline PY - 2004/3/31/entrez SP - 287 EP - 96 JF - Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology JO - Comp Biochem Physiol B Biochem Mol Biol VL - 137 IS - 3 N2 - Two major protease activities were present in gut homogenates of the cladoceran crustacean Daphnia magna: (i) a trypsin activity that hydrolysed the synthetic substrate N-benzoyl-dl-arginine p-nitroanilide and was strongly inhibited by N-p-tosyl-lysine chloroketone (TLCK) and 4-(amidinophenyl)methanesulfonyl fluoride (APMSF) and not inhibited by chymostatin; and (ii) a chymotrypsin activity that hydrolysed synthetic chymotrypsin substrates containing more than one amino acid, did not hydrolyse N-benzoyl-l-tyrosine p-nitroanilide, and was strongly inhibited by chymostatin and not by TLCK and APMSF. Both activities had alkaline pH optima (pH 7-10), but were shown to be due to distinct types of proteases. These two enzyme activities accounted for 75-83% of the proteolytic activity of gut contents. Substrate SDS-polyacrylamide gel electrophoresis revealed nine different proteases ranging from 15 to 73 kDa. SN - 1096-4959 UR - https://www.unboundmedicine.com/medline/citation/15050516/Protease_activity_in_gut_of_Daphnia_magna:_evidence_for_trypsin_and_chymotrypsin_enzymes_ DB - PRIME DP - Unbound Medicine ER -