Purification of human renin substrate
| Autor: | Joseph R. Kahn, Leonard T. Skeggs, Melvin Levine, Kenneth E. Lentz, Frederic E. Dorer |
|---|---|
| Rok vydání: | 1978 |
| Předmět: |
Angiotensins
Size-exclusion chromatography Angiotensinogen Biophysics Kidney Biochemistry Human renin chemistry.chemical_compound Renin Renin–angiotensin system Methods medicine Animals Humans Bioassay Molecular Biology Chromatography Chemistry Electric Conductivity Substrate (chemistry) Cell Biology Hydrogen-Ion Concentration Hydroxylapatite Rats Molecular Weight medicine.anatomical_structure Biological Assay Specific activity Angiotensin I |
| Zdroj: | Analytical Biochemistry. 87:11-18 |
| ISSN: | 0003-2697 |
| DOI: | 10.1016/0003-2697(78)90563-8 |
| Popis: | Renin substrate, angiotensinogen, has been purified from human plasma by methods which permit the processing of large amounts of outdated bank blood. The purified protein is homogeneous by disc gel electrophoresis at pH 9.5. The specific activity of 18 nmol/mg corresponds to a molecular weight of 56,000, while a higher value, 90,000, is found by gel filtration. Chromatography of partially purified renin substrate on DEAE-cellulose in a descending pH gradient shows evidence for the existence of multiple forms. However, some of these forms appear to be lost after chromatography on hydroxylapatite. |
| Databáze: | OpenAIRE |
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