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Multiple forms of angiotensin-converting enzyme in human tissues and fluids
Journal of Clinical Chemistry and Clinical Biochemistry. Zeitschrift Fur Klinische Chemie Und Klinische Biochemie
|July 1, 1985
Summary
This study reveals multiple forms of angiotensin-converting enzyme (ACE) across human tissues using electrophoresis. The developed assay accurately localizes and quantifies ACE activity, aiding in understanding its tissue-specific roles.
Area of Science:
- Biochemistry
- Enzymology
- Molecular Biology
Background:
- Angiotensin-converting enzyme (ACE) plays a crucial role in the renin-angiotensin system.
- ACE exhibits known variations in its biological functions and distribution.
Purpose of the Study:
- To investigate the electrophoretic behavior of ACE in various human tissues and biological fluids.
- To develop and validate a sensitive assay for localizing and quantifying ACE activity.
Main Methods:
- Agar gel and polyacrylamide gel electrophoresis were employed for ACE separation.
- Enzymatic activity was detected using a specific colorimetric reaction.
- Assay specificity was confirmed using captopril and proteinase inhibitors.
Main Results:
- Distinctive tissue-specific differences in ACE electrophoretic patterns were observed.
- Multiple forms of ACE were identified in several human tissues.
- The assay successfully localized ACE in electrophoretograms and estimated total activity.
Conclusions:
- Electrophoresis is a valuable technique for characterizing tissue-specific ACE isoforms.
- The developed assay provides a reliable method for assessing ACE activity and distribution.
- Findings contribute to a better understanding of ACE's role in different physiological contexts.