Literature DB >> 1395509

Serine proteinase inhibitor profiles in the hemolymph of a wide range of insect species.

A Polanowski1, T Wilusz, M S Blum, P Escoubas, J O Schmidt, J Travis.   

Abstract

1. The inhibition of trypsin, chymotrypsin, neutrophil elastase and cathepsin G, and pancreatic elastase by the hemolymph of 14 insect species in six orders has been investigated. 2. All samples showed great diversity in terms of both total proteinase inhibitory capacity and specificity. 3. The highest total inhibitory capacity was found in the larval hemolymph of species in the beetle family Tenebrionidae and the lowest in that of an adult coreid bug, Acanthocephala femorata.

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Year:  1992        PMID: 1395509     DOI: 10.1016/0305-0491(92)90075-3

Source DB:  PubMed          Journal:  Comp Biochem Physiol B        ISSN: 0305-0491


  2 in total

1.  NMR solution structure of Apis mellifera chymotrypsin/cathepsin G inhibitor-1 (AMCI-1): structural similarity with Ascaris protease inhibitors.

Authors:  T Cierpicki; J Bania; J Otlewski
Journal:  Protein Sci       Date:  2000-05       Impact factor: 6.725

2.  Skin irritation and potential antioxidant, anti-collagenase, and anti-elastase activities of edible insect extracts.

Authors:  Kankanit Yeerong; Suwannee Sriyab; Suvimol Somwongin; Chanun Punyoyai; Panuwan Chantawannakul; Songyot Anuchapreeda; Adchara Prommaban; Wantida Chaiyana
Journal:  Sci Rep       Date:  2021-11-25       Impact factor: 4.379

  2 in total

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