Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung.

  title={Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung.},
  author={David W. Cushman and Herman S. Cheung},
  journal={Biochemical pharmacology},
  volume={20 7},

A Reliable Radiometric Assay for the Determination of Angiotensin I-Converting Enzyme Activity in Urine

Comparison of dialysis and ultrafiltration for concentration of urine showed the existence of angiotensin-converting enzyme inhibitors in human urine, and the kidney tubular epithelial origin of the enzyme is confirmed.

Simplified enzymatic assay of angiotensin-converting enzyme in serum.

The proposed method features coupling an established reaction catalyzed by gamma-glutamyltransferase to the ACE reaction, which releases glycylglycine from the artificial substrate hippuryl-glycyl- glycine, which becomes rate-limiting in the GGT reaction.

Sensitive fluorimetric assay for serum angiotensin-converting enzyme with the natural substrate angiotensin I.

The assay of serum angiotensin-converting enzyme is of use in the diagnosis and possible management of sarcoidosis and Gaucher's disease, and may have other applications.

Human lung angiotensin converting enzyme. Purification and antibody preparation.

Antibody to human lung angiotensin converting enzyme has permitted tissue localization of the enzyme, which appears to be clinically useful in diseases associated with abnormal abundance of angiotENSin-converting enzyme in tissues, such as sarcoidosis.

Inhibitor binding assay for angiotensin-converting enzyme.

The novel assay principle presented here is simple and specific, and can be extended to use with various biological fluids and tissues, and to other enzymes as well.

A fluorimetric assay for angiotensin-I converting enzyme in human serum.




A rapid simple method for the assay of renin in rabbit plasma.

The assay is sufficiently sensitive to measure renin in the plasma of all normal rabbits and can be extended to measure much lower activities, such as the percentage release of the angiotensin content/hr.

Activity of Various Fractions of Bradykinin Potentiating Factor against Angiotensin I Converting Enzyme

The venom from Bothrops jararaca contains enzymes which liberate kinins from plasma kininogen and a peptidic fraction which potentiated the actions of bradykinin on various isolated organs and on the blood pressure of the cat.

Conversion of Angiotensin I to Angiotensin II by Cell-free Extracts of Dog Lung

This communication describes some of the enzymes in extracts of dog lung that metabolize angiotensins I and II and particularly those catalysing the conversion ofAngiotensin I to angiotENSin II (“converting enzyme”) and the enzyme(s) responsible for the inactivation of ang Elliotensin II and angiotsin I are referred to as “destroying enzyme’.

A modified spectrophotometric determination of chymotrypsin, trypsin, and thrombin.

  • B. C. Hummel
  • Biology, Chemistry
    Canadian journal of biochemistry and physiology
  • 1959
The spectrophotometric procedure proposed by Schwert and Takenaka has been modified and extended to include the application to N-benzoyl-L-tyrosine ethyl ester and α-p-toluenesulphonyl- L-arginine methyl ester, allowing the determination of traces of chymotrypsin in the presence of relatively large amounts of trypsin.