Serine proteinase inhibitor profiles in the hemolymph of a wide range of insect species.
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.
Polanowski
A
A
Institute of Biochemistry, Wroclaw University, Poland.
Wilusz
T
T
Blum
M S
MS
Escoubas
P
P
Schmidt
J O
JO
Travis
J
J
D000595:Amino Acid Sequence; D000818:Animals; D056649:Cathepsin G; D002403:Cathepsins / Q000037:antagonists & inhibitors; D002918:Chymotrypsin / Q000037:antagonists & inhibitors; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000378:metabolism; D006458:Hemolymph / Q000201:enzymology*; D007313:Insecta / Q000201:enzymology*; D008969:Molecular Sequence Data; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors; D012697:Serine Endopeptidases; D015842:Serine Proteinase Inhibitors / Q000378:metabolism / Q000502:physiology*; D014361:Trypsin Inhibitors / Q000502:physiology
D015842:Serine Proteinase Inhibitors; D014361:Trypsin Inhibitors; D002403:Cathepsins; D010450:Endopeptidases; D012697:Serine Endopeptidases; D002918:Chymotrypsin; D056649:Cathepsin G; D010196:Pancreatic Elastase