Un substrat pour le dosage chimique de la rénine

Roth, Marc; Reinharz, A.

doi:10.1002/hlca.19660490625

Cited by 14 publications

(7 citation statements)

References 7 publications

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“…However, a very timely report came out from Roth's laboratory in Geneva, Switzerland. Roth and Reinharz 18 had synthesized a fluorogenic substrate for renin and a simple method for fluorometric determination of renin activity was devised. 19 This method was to become the critical factor in the purification of renin.…”

Section: Auynlmarkmentioning

confidence: 99%

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Purification of renin and prorenin.

Inagami

1991

Hypertension

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Section: Auynlmarkmentioning

confidence: 99%

“…These include discovery of renin-like activity in the male mouse submandibular gland, 14 pepstatin, 24 affinity chromatography, 30 selective extraction method, 35 fluorogenic renin substrate, 18 radioimmunoassay, 37 and introduction of protease inhibitors.…”

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confidence: 99%

Purification of renin and prorenin.

Inagami

1991

Hypertension

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“…Previously published procedures were utilized for the synthesis of Z-Pro-Phe-HisLeu-Leu-Val-Tyr-Ser-ß-naphthylamide and Z-Val-Tyr-Ser-ß-naphthylamide [1], and of Z-Leu-Leu-ß-naphthylamide, Z-Leu-Val-Tyr-Ser-ß-naphthylamide and ZPro-Phe-His-Leu-ß-naphthylamide [2],…”

Section: Methodsmentioning

confidence: 99%

“…In previous publications [1,2] we reported the synthesis and use of an artificial octapeptide substrate of renin (EC 3. 4.…”

Section: Introductionmentioning

confidence: 99%

Studies on Pituitary Catkepsin D with Artificial Substrates

Reinharz¹,

Roth²

1971

Enzyme

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A proteolytic enzyme acting at acidic pH has been partially purified from bovine anterior pituitary. It was found to hydrolyze the artificial substrate, Z-Pro-Phe-His-Leu-Leu-Val- Tyr-Ser-ß-naphthylamide at the Phe-His and the Leu-Leu bonds. This hydrolysis serves as basis of a sensitive fluorimetrie assay. The enzyme is similar to cathepsin D. The pentapeptides Z-Pro- Phe-His-Leu-Leu-β-naphthylamide and Z-Leu-Leu-Val-Tyr-Serß- naphthylamide were also attacked, but at a much slower rate. Smaller substrates were not hydrolyzed. The results indicate that the enzyme preferentially hydrolyzes peptide bonds involving the carboxyl group of an hydrophobic amino acid.

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“…EDTA (tetrasodium salt), sulfanilic acid, acetic anhydride, iodine, sodium nitrite and potassium iodide were reagent grade products from Merck (Darmstadt, Germany). The fluorigenic substrate, Z-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser-ß naphthylamide, was synthesized as described earlier [1].…”

Section: Reagentsmentioning

confidence: 99%

Effect of some Chemical Agents on Renin Activity in vitro

Reinharz¹,

Roth²,

Haefeli³

et al. 1971

Enzyme

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The effect of different chemical reagents on renin has been investigated. After treatment of hog renin with acetic anhydride, 1-fluoro-2,4-dinitrobenzene, diazobenzene sulfonic acid and phenyl isocyanate, the enzymic activity assayed both biologically and chemically was depressed, whereas no effect occurred after treatment with diisopropyl fluorophosphate, p-chloromercuribenzoate and after dialysis against EDTA. Human renin, too, is inactivated by acetylation, diazo coupling and dinitrobenzoylation. The results indicate that one or several amino groups of the renin molecule are essential for enzymic activity.

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Un substrat pour le dosage chimique de la rénine

Abstract: Volumem 49, Fasciculus 6 (1966) -No. 225 1903 225. Un substrat pour le dosage chimique de la rknine par M. Roth et Anja Reinharz (14 VI 66)

Cited by 14 publications

References 7 publications

Purification of renin and prorenin.

Purification of renin and prorenin.

Studies on Pituitary Catkepsin D with Artificial Substrates

Effect of some Chemical Agents on Renin Activity in vitro

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