hymenolepis/arginine

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Hymenolepis diminuta: interactions of the isolated brush border membrane with proteolytic enzymes.

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Proteins of the isolated brush border membrane of Hymenolepis diminuta were hydrolyzed in vitro by chymotrypsin, papain, pepsin, subtilopeptidase A (= subtilisin Carlsberg), and trypsin. Neither proteolytic nor amidase activity was demonstrable in the isolated membrane using proteinaceous (casein

A radiometric analysis of nitric oxide synthase activity in Hymenolepis diminuta.

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The free radical nitric oxide (NO) is a neuronal messenger which is synthesized from L-arginine and O2 by nitric oxide synthase (NOS). In the synthesis NO and L-citrulline are produced in a stoichiometric 1:1 relation. The activity of NOS was analysed in homogenates of the rat tapeworm Hymenolepis

A serine proteinase in the penetration glands of the hexacanths of Hymenolepis diminuta (Cestoda, Cyclophyllidea).

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Histochemically demonstrable activity of a serine proteinase was detected in the penetration glands of Hymenolepis diminuta hexacanths. At the optimal pH of 8.4 the enzyme hydrolyzed N-blocked L-aminoacyl- and N-blocked L-peptidyl-naphthylamides bearing L-arginine at the P1 subsite. The proteinase

Trypsin inactivation by intact Hymenolepis diminuta (Cestoda): some characteristics of the inactivated enzyme.

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In the presence of intact Hymenolepis diminuta, trypsin was inactivated; intact worms had no apparent effect on subtilisin, pepsin, or papain. Inactivation of trypsin was demonstrable using azoalbumin as a substrate, but the inactivated enzyme retained full catalytic activity against

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