| Autor: |
Smillie, L. B., Mabbott, G. Y., Neufeld, G. R. |
| Zdroj: |
Canadian Journal of Physiology and Pharmacology; May 1962, Vol. 40 Issue: 5 p555-564, 10p |
| Abstrakt: |
The purification of trypsinogen by several methods of ion-exchange chromatography has been investigated. The use of phosphate–urea buffers on Bio-Rex 70 was not a suitable preparative procedure because of considerable inactivation of the zymogen. Chromatography on carboxymethyl cellulose at pH 3.2 produced no significant increase in the potential tryptic activity. In the presence of soybean trypsin inhibitor, trypsinogen was successfully chromatographed on Bio-Rex 70 to yield a product of high potential activity and of low free tryptic and chymotryptic activity. It was essentially free from soybean trypsin inhibitor and possessed the physical parameters previously published for this protein. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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