| Autor: |
N M, Modesti, C E, Argaraña, H S, Barra, R, Caputto |
| Rok vydání: |
1984 |
| Předmět: |
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| Zdroj: |
Journal of neuroscience research. 12(4) |
| ISSN: |
0360-4012 |
| Popis: |
When a 25-50% ammonium-sulphate-insoluble fraction from a bovine brain preparation was chromatographed on a cellulose phosphate column, several protein fractions which inhibit the activity of tubulinyl-tyrosine carboxypeptidase were obtained. One of these fractions exhibited activity of fructose-bisphosphate aldolase (EC 4.1.2.13) and the enzyme accounted for more than 95% of the protein of this fraction as judged by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The inhibitory activities of the two protein fractions which had the highest activity per mg of protein were practically abolished by pretreatment with pronase; preincubation with trypsin, on the other hand, caused only a partial inactivation of the inhibitors. The inhibitory activities were little affected by heating at 90 degrees C for 5 min. Preincubation with purified tubulinyl-tyrosine carboxypeptidase caused a great decrease of the inhibitory activities of these two fractions, leaving open the possibility that these inhibitors act as substrates of the carboxypeptidase. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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