peregrina/protease

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Antibacterial activity of a novel 26-kDa serine protease in the yellow body of Sarcophaga peregrina (flesh fly) pupae.

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We have reported a novel serine protease produced by Sarcophaga peregrina (Nakajima et al., J. Biol. Chem. 272 (1997) 23805-23810). This 26-kDa protease showed antibacterial activity against several bacteria. This activity was an intrinsic characteristic of the enzyme protein and not directly

Identification and characterization of an antibacterial peptide of the 26-kDa protease of Sarcophaga peregrina with antibacterial activity.

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Previously, we purified a serine protease with a molecular mass of 26 kDa that exhibits potent antibacterial activity from a pupal extract of Sarcophaga peregrina (flesh fly). We divided this protease into 12 peptides and examined their antibacterial activity. A peptide corresponding to residues 155

Purification and characterization of an inhibitor of the cysteine protease from the hemolymph of Sarcophaga peregrina larvae.

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The hemolymph of Sarcophaga peregrina (flesh fly) larvae was found to contain multiple inhibitors of hemocyte cysteine protease. One of them, named sarcocystatin A, was purified and found to be a mixture of the components sarcocystatin A alpha and A beta in a molar ratio of 2:1. These components can

A novel protease in the pupal yellow body of Sarcophaga peregrina (flesh fly). Its purification and cDNA cloning.

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We purified a novel serine protease with a molecular mass of 26 kDa from Sarcophaga pupae. This protease appeared almost exclusively in the yellow body, an organ that develops temporarily in the pupae of dipteran insects and expands to form the adult midgut by engulfing the larval midgut. cDNA

[Proteases participating in metamorphosis of flesh fly (Sarcophaga peregrina)].

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