Literature DB >> 8817875

Purification and assay methods for angiotensin-converting enzyme.

Q C Meng1, S Oparil.   

Abstract

Angiotensin-converting enzyme (ACE; EN 3.4.15.1) is a peptidyl dipeptide hydrolase that removes the carboxyl terminal His-Leu from angiotensin I to produce the octapeptide angiotensin II. In addition, ACE inactivates bradykinin, a vasodilator peptide/mediator of inflammation, as well as substance P, enkephalins and endorphins. Because of the importance of ACE and its active site-directed inhibitors in the pathogenesis and treatment of cardiovascular disorders such as hypertension and heart failure, ACE purification and assay are of clinical and commercial, as well as scientific interest. This review summarizes the historical development of ACE purification and assay methods and presents some innovative high-performance liquid chromatography-based techniques developed in our own laboratory for high yield and efficient purification and sensitive and specific assay of ACE.

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Year:  1996        PMID: 8817875     DOI: 10.1016/0021-9673(96)00372-x

Source DB:  PubMed          Journal:  J Chromatogr A        ISSN: 0021-9673            Impact factor:   4.759


  3 in total

1.  Purification of Angiotensin-Converting Enzyme (ACE) from Sheep Kidney and Inhibition Effect of Reduced Nicotinamide Adenine Dinucleotide (NADH) on Purified ACE Activity.

Authors:  Aysenur Kiylik; Vedat Turkoglu; Zehra Bas
Journal:  Cell Biochem Biophys       Date:  2021-10-07       Impact factor: 2.194

Review 2.  Macroalgal Proteins: A Review.

Authors:  Ronan O' Brien; Maria Hayes; Gary Sheldrake; Brijesh Tiwari; Pamela Walsh
Journal:  Foods       Date:  2022-02-16

3.  Purification and characterization of angiotensin-converting enzyme (ACE) from sheep lung.

Authors:  Fatih Aydin; Vedat Turkoglu; Zehra Bas
Journal:  Mol Biol Rep       Date:  2021-06-04       Impact factor: 2.316

  3 in total

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