Isolierung von Bradykinin aus Rinderplasma nach Einwirkung von Schlangengift <i>(Bothrops jararaca)</i>. Vorläufige Mitteilung

Zuber, Herbert; Jaques, R.

doi:10.1002/hlca.19600430422

Cited by 37 publications

(4 citation statements)

References 9 publications

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“…And finally, the threshold dose of pure natural snake-venom-bradykinin (1 ng./ml.) for contraction of the isolated guinea-pig ileum (Zuber and Jaques, 1960) is identical with the threshold dose of nonapeptide A in this organ.…”

Section: Efjects On Capillary Permeabilitymentioning

confidence: 62%

“…As in the case of bradykinin and of nonapeptide A the rat uterus was more sensitive (approximately 20times) than the guinea-pig ileum to octapeptide B. Boiling with concentrated hydrochloric acid or incubating with guinea-pig serum abolishes the action of octapeptide B on the isolated guinea-pig ileum. This octapeptide B, however, is markedly less potent (50 to 100 times) in various tests (isolated guinea-pig ileum, isolated rat uterus, tidal air of anaesthetized guinea-pigs) than pure trypsinbradykinin (Elliott, Horton, and Lewis, 1960) and pure snake-venom-bradykinin (Zuber and Jaques, 1960). It is thus definitely not identical with them.…”

Section: Efjects On Capillary Permeabilitymentioning

confidence: 92%

“…It is, however, remarkable that recently after isolation of a bradykinin resulting from the action of snake-venom on bovine plasma, Zuber and Jaques (1960) have stated that this snake-venombradykinin in an essentially pure form contains the five amino acids arginine, phenylalanine, proline, glycine, and serine in the ratio of 2:2:2: 1: 1. It therefore corresponds to the amino acid composition found for trypsin-bradykinin by Elliott, Lewis, and Horton (1960a).…”

Section: Efjects On Capillary Permeabilitymentioning

confidence: 99%

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Biological Activity of Synthetic Polypeptides With Bradykinin‐like Properties

Konzett

Stürmer²

1960

British Journal of Pharmacology and Chemotherapy

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The biological activity of synthetic polypeptides containing the amino acids of natural pure trypsin-bradykinin and snake-venom-bradykinin has been investigated. A series of tests for bradykinin-like activity in stimulating plain muscle, depressing the blood pressure and increasing capillary permeability was used on various species. A nonapeptide with the following structure: -Arg-OH also exerted bradykinin-like effects but was 50 to 100 times less active than the nonapeptide. Three other octapeptides and a heptapeptide were without any significant effect. Further work will demonstrate if the nonapeptide A is synthetic bradykinin or a peptide with bradykinin-like activity.Note added since submission of this paper: The data from this investigation were personally precommunicated to Elliott, Lewis, and Horton, who have since found that the structure of pure trypsin-bradykinin is identical with the structure of the nonapeptide A. Therefore, this synthetic nonapeptide is in fact synthetic bradykinin.Since the discovery of bradykinin, its polypeptide nature has been suggested and amply verified (Rocha e Silva, Beraldo and Rosenfeld, 1949; Rocha e Silva, 1955Silva, , 1960. The amino acid composition of bradykinin prepared by the action of trypsin on the fraction of ox plasma precipitating between 35 and 45% of saturation by ammonium sulphate (trypsin-bradykinin) was recently studied by Elliott, Lewis, and Horton (1960a) following its isolation; according to these investigators the molecule of trypsin-bradykinin contains two moles each of arginine, phenylalanine, and proline, and one mole each of TABLE I

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Section: Efjects On Capillary Permeabilitymentioning

confidence: 62%

Section: Efjects On Capillary Permeabilitymentioning

confidence: 92%

Section: Efjects On Capillary Permeabilitymentioning

confidence: 99%

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Biological Activity of Synthetic Polypeptides With Bradykinin‐like Properties

Konzett

Stürmer²

1960

British Journal of Pharmacology and Chemotherapy

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“…Many peptidases are known to inactivate bradykinine.g., kininase I and II in the blood (Yang and Erd6s, 1967), post-proline cleaving enzymes in sheep kidney (Koida and Walter, 1976) and in rabbit brain (Orlowski et al, 1979), kininase A and B in rabbit brain (Oliveira et al, 1976), and pancreatic carboxypeptidase A (EC 3.4.12.2) and B (EC 3.4.12.3) (Zuber and Jaques, 1960).…”

Section: Resultsmentioning

confidence: 99%

Properties of Kininase in Rat Dental Pulp

Maita¹,

Endo

Ogura

1984

J Dent Res

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A kininase, capable of degrading bradykinin, was partially purified from the dental pulp of rats, and its properties were investigated. Chromatography on both Sephadex G-200 and DEAE Sephadex A-50 columns gave a single peak of kininase activity. The molecular weight of the enzyme, estimated by gel filtration, was about 67,000, and the optimum pH for the enzymatic reaction was about 7.5. The enzyme appears to contain a labile SH group(s) that is essential for its activity, because CdCl2, HgCl2 (0.1 mM each), and p-chloromercuric benzoate (0.05 mM) inhibited the enzyme completely, while dithiothreitol retarded the loss of activity during storage. Of various peptides tested, bradykinin was the substrate most sensitive for the enzyme. The enzyme released several amino acids located in the C-terminal regions of bradykinin--angiotensin I and neurotensin--but only one C-terminal amino acid from des-Arg9--bradykinin and angiotensin II. In contrast, the enzyme did not release any amino acids from substance P, of which only the two amino acids in the N-terminal region are the same as those of bradykinin, but its C-terminal is blocked by an amino group. Although the enzyme was not so highly purified as to rule out the contribution of other peptidases, these results suggest that the dental pulp of rats may contain a single enzyme that degrades bradykinin, and the enzyme may be a type of carboxypeptidase, differing from known kininases from other animal sources.

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Synthese von L‐Arginyl‐L‐propyl‐L‐propyl‐glycyl‐L‐phenylalanyl‐L‐seryl‐L‐phenylalanyl‐L‐arginin (Bradykinin?). Vorläufige Mitteilung

Schwyzer

Rittel

Sieber

et al. 1960

Helvetica Chimica Acta

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1130HELVETICA CHIMICA ACTA rnit Essigester). Rf-Wert in n-Butanol-Eisessig-Wasser (4: 1 : 5) = 0,7 (i. Vgl. Dinitrophenylarginin 0,6), Nach der Totalhydrolyse wurde Dinitrophenyl-arginin gefunden (Arginin ist NH ifber diese Arbeiten, die im Rahmen unserer Studien fiber Po1ypeptid-Wirkstoffel2) durchgefiihrt wurden, sol1 spater eingehender berichtet werden. SUMMARYBradykinin, resulting from the action of snake venom (Bothofis jararaca) on bovine plasma, has been isolated in an essentially pure form. It contains the five amino acids arginine, phenylalanine, proline, glycine and serine in the ratio of 2 : 2 : 2 : 1 : I, corresponding to the amino acid composition found for bradykinin stemming from the action of trypsin on corresponding plasma proteins. Degradation studies give the following partial sequence : H .Arg-(Pro,, Gly, Ser, Phe)-Phe-Arg. OH. Synthese von

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Isolierung von Bradykinin aus Rinderplasma nach Einwirkung von Schlangengift (Bothrops jararaca). Vorläufige Mitteilung

Cited by 37 publications

References 9 publications

Biological Activity of Synthetic Polypeptides With Bradykinin‐like Properties

Biological Activity of Synthetic Polypeptides With Bradykinin‐like Properties

Properties of Kininase in Rat Dental Pulp

Synthese von L‐Arginyl‐L‐propyl‐L‐propyl‐glycyl‐L‐phenylalanyl‐L‐seryl‐L‐phenylalanyl‐L‐arginin (Bradykinin?). Vorläufige Mitteilung

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