Substrates for angiotensin converting enzyme

Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving hydrolase

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424 15, C12Q 136

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active

042516285

ABSTRACT:
A method is disclosed for quantitative measurement of angiotensin converting enzyme activity in biological material. The method exploits certain acylated tripeptide substrates. The enzyme-catalyzed hydrolysis of the substrates results in the formation of a dipeptide reaction product and a remnant product. The substrate is radioactively labeled exclusively in that portion destined to become the remnant product. Preferably, the substrate prior to hydrolysis is essentially insoluble in an aprotic organic solvent, but the remnant hydrolysis product is essentially quantitatively extractible by the organic solvent. At the termination of the enzyme-catalyzed hydrolysis, the labeled remnant product is separated from the reaction mixture, and the radioactivity is counted in a suitable apparatus.

REFERENCES:
patent: 3832337 (1974-08-01), Ondetti et al.
patent: 4041147 (1977-08-01), Pagnucco et al.
patent: 4057629 (1977-11-01), Miki et al.
patent: 4115374 (1978-09-01), Ryan et al.
Chiu et al., "A Sensitive Radiochemical Assay for Angiotensin-Converting Enzyme (Kinase 11)", Biochem. J. vol. 149, (1975), pp. 297-300. _
Dorer et al., "Kinetic Properties of Pulmonary Angiotensin-Converting Enzyme. Hydrolysis of Hippurylglycylglycine", Biochim. Biophys. Acta., vol. 429 (1976) pp. 220-228. _
Erdos, "Conversion of Angiotensin I to Angiotensin II", Am. J. Med., (1976) vol. 60, pp. 749-758. _

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