chymotrypsin/edema

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[Therapeutic trials of a trypsin-alpha-chymotrypsin combination in edema of venous origin and hydrolipopexia].

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An experimental evaluation of the efficacy of chymotrypsin in the reduction of edema in crushed extremities.

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[SIMPLIFIED PHARMACOLOGICAL METHOD OF STUDY OF INDUCED INFLAMMATORY EDEMA: ITS APPLICATION TO A MUCOPOLYSACCHARIDASE-ALPHA-CHYMOTRYPSIN COMBINATION].

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The use of chymotrypsin to decrease postoperative edema in abrasive surgery.

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[Contribution to the treatment of hematomas and edemas with alpha-chymotrypsin].

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[A double-blind study of an association of mucopolysaccharidases and of alpha-chymotrypsin (alphamucase) in the prevention and treatment of postoperative edema].

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Effects of intracameral administration of α-chymotrypsin on intracapsular lens extraction and postoperative outcome in clinically normal dogs.

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OBJECTIVE To assess the intraoperative and postoperative clinical effects and histologic effects of intracameral administration of α-chymotrypsin in clinically normal dogs undergoing standard intracapsular lens extraction (ICLE). METHODS 6 young adult male dogs without evidence of systemic or ocular

The chymotrypsin-sensitive site, FFD315, in anthrax toxin protective antigen is required for translocation of lethal factor.

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The protective antigen (PA) component of anthrax toxin contains two sites that are uniquely sensitive to proteolytic cleavage. Cleavage at the sequence RKKR167 by the cellular protease furin is absolutely required for toxicity, whereas cleavage by chymotrypsin or thermolysin at the sequence FFD315

The amino acid sequence and properties of an edema-inducing Lys-49 phospholipase A2 homolog from the venom of Trimeresurus mucrosquamatus.

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Three phospholipase A2 enzymes or homologs were purified from the venom of Trimeresurus mucrosquamatus (Taiwan habu). The most abundant one was found to be a phospholipase homolog without enzyme activity, and its complete amino acid sequence was determined using oligopeptide fragments derived from

Rat paw edema induced by trimucase II, a kinin-releasing enzyme from Trimeresurus mucrosquamatus venom.

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Trimucase II, a proteolytic enzyme isolated from Trimeresurus mucrosquamatus venom, caused rat hind-paw edema dose dependently. Captopril potentiated significantly, while pretreatment with cellulose sulfate suppressed the trimucase II-induced edematous response. Pretreatment with diphenhydramine and

Leucaena leucocephala serine proteinase inhibitor: primary structure and action on blood coagulation, kinin release and rat paw edema.

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A serine proteinase inhibitor isolated from Leucaena leucocephala seeds (LlTI) was purified to homogeneity by acetone fractionation, ion exchange chromatography, gel filtration and reverse phase chromatography (HPLC). SDS-PAGE indicated a protein with M(r) 20000 and two polypeptide chains

Amblyomma americanum serpin 41 (AAS41) inhibits inflammation by targeting chymase and chymotrypsin.

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Ticks inject serine protease inhibitors (serpins) into their feeding sites to evade serine protease-mediated host defenses against tick-feeding. This study describes two highly identitical (97%) but functionally different Amblyomma americanum tick saliva serpins (AAS41 and 46) that are secreted at

Pentoxifylline attenuates edema formation in proteolytic enzyme-induced lung injury.

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Ex vivo canine lung lobes were exposed to a pancreatic proteolytic enzyme (chymotrypsin) alone or chymotrypsin after pretreatment with a continuous infusion with pentoxifylline. The lobes exposed to chymotrypsin gained 133 g, while the pentoxifylline-treated lobes gained only 65 g (p less than .05)

Identification of a salivary vasodilator in the primary North American vector of bluetongue viruses, Culicoides variipennis.

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Several species of Culicoides biting midges are important pests and vectors of pathogens affecting humans and other animals. Bluetongue is the most economically important arthropod-borne animal disease in the United States. Culicoides variipennis is the primary North American vector of the

A histopathological study of pancreatic lesions after chronic administration of methamphetamine to rats.

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The effects of chronic administration of methamphetamine on pancreatic tissues were histopathologically studied in experimental models. Methamphetamine (1 ml/kg body weight/day) was subcutaneously injected into 14 five-week-old male Wistar Kyoto rats (WKY) for 12 weeks. Age and sex matched 5 WKY

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