No abstract

Can. Ent. 116: 1393-1396 (1984) The posterior midgut of a seed-feeding pentatomid, Euschistus euschistoides (Vollenhoven), contains the proteinases cathepsin B and aminopeptidase. Cathepsin B hydrolysis of benzoyl-DL-arginine-2-naphthylamide is activated by thiol chemicals and EDTA. Aminopeptidase hydrolysis of leucine-p-nitroanilide is activated by MgC1, and inhibited by cysteine, glutathione, EDTA, and CaCI,. These results are similar to those obtained for cathepsin B and aminopeptidase from blood-feeding Hemiptera and support the hypothesis that catheptic proteinases are unique to this order. ResumeLe mksentkron postkrieur du pentatomide granivore Euschistus euschistoides (Vollenhoven) contient les protkinases cathepsine B et l'aminopeptidase. L'hydrolyse du benzoyl-DL-arginine-2-naphthylamide par la cathepsine B est activke par les produits de type thiol et par I'EDTA. L'hydrolyse de la leucine-p-nitroanilide par I'aminopeptidase est activke par le MgCI, et inhibke par la cystkine, le glutathione, I'EDTA et le CaCI,. Ces rksultats sont semblables h ceux obtenus avec la cathepsine B et I'aminopeptidase provenant d'hkmiptkres hkmatophages, appuyant I'hypothkse voulant que les proteinases catheptiques sont uniques B cet ordre.

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Bis (3-chloro-4-dodecyloxyphenyl) malondialdehyde copper(II), as well as its nickel(II) homologue have been synthesised. The copper(II) complex shows a narrow (15 °C) nematic phase below its clearing temperature. The nickel(II) complex is polymeric in nature.

ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.