| Autor: |
Abdulazeez, M. A., Kurfi, B. G. |
| Předmět: |
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| Zdroj: |
Bayero Journal of Pure & Applied Sciences; 2016, Vol. 9 Issue 2, p24-29, 6p |
| Abstrakt: |
Angiotensin converting enzyme (ACE) was isolatedand partially purified from the lungs of Wistarrats (Rattusnorvegicus). The ACE was characterized and its amino acids composition determined. ACE was purified by ammonium sulphate precipitation, dialysis and gel filtration chromatography. The activity of the enzyme was assayed by a spectrophotometry method, which involves monitoring the rate of production of hippuric acid from the hydrolysis of Hippuryl-L-Histidyl-L-Leucine by ACE. Protein concentration was assayed by Biuret method; amino acid content, optimum temperature and pH of the isolated enzyme were also determined. From the results, the crude enzyme had a total activity of 0.12 U and a specific activity of 0.048U/mg of protein. Precipitation of protein increased the specific activity to 0.050U/mg at a recovery rate of 62%. Upon dialysis, the activity of the enzyme decreased from 0.074U to 0.038U while specific activity also increased. At this stage, only about 31% of the enzyme activity was retained over the crude. After gel filtration the specific activity of the enzyme increased to 0.087U/mg at a purification fold of 1.8 and a final recovery of 25%.The enzyme had an optimum pH and temperature of 7.0 and 40°C, respectively. The partially purified enzyme is an oligopeptide having seventeen amino acids:KHRDTSGPGACVMILYF. In conclusion, this study has shown that angiotensin-converting enzyme can be isolated from rat lungs, but the purification steps needs to be modified to obtain an enzyme with higher yield and specific activity that will be easily assessable for research in developing countries. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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