Trasylol

Trautschold, I.; Werle, E.; Zickgraf-Rüdel, Gertrud

doi:10.1016/0006-2952(67)90186-4

Cited by 107 publications

(43 citation statements)

References 50 publications

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“…To analyse this possibility, virus polypeptide synthesis in the presence of protease inhibitors was studied. The following inhibitors were used: TLCK, a trypsin inhibitor (Shaw et al, 1965), TPCK, a chymotrypsin inhibitor (Schoellmann & Shaw, 1963) and inhibitors of trypsin-and chymotrypsin-like proteases, phenylmethylsulphonyl fluoride (PMSF; Gold, 1965) and aprotinin [Gordox ®, Gedeon Richter, Hungary (Trautschold et al, 1967)]. The intracellular cleavage of human influenza virus NP was found to be effectively inhibited by TPCK and less by TLCK.…”

Section: Short Communicationmentioning

confidence: 99%

Nucleoproteins of Animal Influenza Viruses, in Contrast to Those of Human Strains, Are Not Cleaved in Infected Cells

Жирнов

Bukrinskaya

1984

Journal of General Virology

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Section: Short Communicationmentioning

confidence: 99%

Nucleoproteins of Animal Influenza Viruses, in Contrast to Those of Human Strains, Are Not Cleaved in Infected Cells

Жирнов

Bukrinskaya

1984

Journal of General Virology

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“…Preliminary results (Di Rosa & Sorrentino, 1968) indicated that aprotinin, the well known protease inhibitor (Trautschold, Werle & Zickgraf-Rudel, 1967), depressed the carrageenin oedema and showed the ability of carrageenin to release kinin-like substance(s) from plasma substrates.…”

Section: Introductionmentioning

confidence: 99%

Some pharmacodynamic properties of carrageenin in the rat

Rosa

Sorrentino

1970

British J Pharmacology

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Summary1. Carrageenin oedema is suppressed by pre-treating the rats with cellulose sulphate, a kininogen depleting agent. This inhibition is closely related to the dose of cellulose sulphate and to the time course of kininogen depletion. 2. Oedema induced by egg white or by dextran, in which the mediators are histamine and 5-hydroxytryptamine, is quite unaffected by cellulose sulphate treatment. 3. Carrageenin injected intravenously lowers the arterial blood pressure of rats. This hypotensive effect is unaffected by histamine antagonists and is abolished by protease inhibitors and thus seems to be due to kinin release from plasma substrates. 4. Like cellulose sulphate, carrageenin enhances the esterolytic activity of the blood from treated rats when incubated with benzoyl-arginine ethyl ester. 5. The ability of carrageenin to activate the kinin-forming system could account for both its inflammatory and hypotensive effects.

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“…There is evidence for structural alteration of aprotinin in the liver and in renal tissue (see Trautschold et al, 1967;Werle, 1970). Another possible explanation of the results is that aprotinin prevents replacement of kininase in the circulation.…”

Section: Discussionmentioning

confidence: 94%

“…It inhibits enzymes of different substrate specificity, such as trypsin, chymotrypsin, various kallikreins, plasmin and some undefined cell proteinases (Trautschold, Werle & Zickgraf-Rudel, 1967). Its activity is expressed in terms of kallikrein inhibitor units (KIU) and 1 KIU (0-14-015 ,ug) is the amount of inhibitor which produces 50% inhibition of 2 kallikrein units (KU) under standard conditions in vitro (incubation for 30 min at pH 8 and 370 C; Werle & Kaufmann-Boetsch, 1960).…”

Section: Introductionmentioning

confidence: 99%

“…Aprotinin is less well tolerated in rats, especially when they have undergone surgery. High doses in rats may lead to fatal 'shock-like reactions' (see Trautschold et al, 1967). Occasionally, repeated high doses in patients with a history of allergy have led to ' signs of intolerance' (see Trautschold et al, 1967), probably due to histamine release (Haberland, 1967).…”

Section: Introductionmentioning

confidence: 99%

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Inhibitory effects of aprotinin on kallikrein and kininases in dog's blood

Pojda

Vane

1971

British J Pharmacology

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Summary The blood‐bathed organ technique was used in dogs to estimate kinin generation in the blood. Strips of cat jejunum were used as assay tissues. Infusions of kallikrein at 0·5–8 mu/ml into the blood in the extracorporeal circuit led to a generation of kinin at 0·6–10 ng/ml. The kinin generated was at the same concentration after incubation of kallikrein with blood for 15 s or 120 seconds. Intravenous infusions of kallikrein at (8–125 mu/kg)/min led to similar blood concentrations of kinin. These infusions induced substantial falls in blood pressure. Aprotinin inhibited the generation of kinin by kallikrein, but the concentration needed in vivo was 20,000 times higher than would be expected from the definition of the units. After intravenous injection of large doses of aprotinin, the kallikrein‐inhibiting activity passed off within 40–60 minutes. At the same time, there was a gradual reduction in kininase activity, so that the half life of bradykinin in blood increased from a mean of 13 s to 40 seconds. This effect reached a maximum 1–3 h after injection of aprotinin. It is suggested that a metabolite of aprotinin is responsible for the kininase inhibition and that this effect may limit the usefulness of aprotinin in man.

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Trasylol

Cited by 107 publications

References 50 publications

Nucleoproteins of Animal Influenza Viruses, in Contrast to Those of Human Strains, Are Not Cleaved in Infected Cells

Nucleoproteins of Animal Influenza Viruses, in Contrast to Those of Human Strains, Are Not Cleaved in Infected Cells

Some pharmacodynamic properties of carrageenin in the rat

Inhibitory effects of aprotinin on kallikrein and kininases in dog's blood

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