Purification and some properties of buffalo spleen cathepsin Β.
| dc.contributor.author | Ahmad, Sarfraz | |
| dc.contributor.author | Agarwal, Sudhir K | |
| dc.contributor.author | Khan, M Yahiya | |
| dc.date.accessioned | 2015-07-28T06:09:14Z | |
| dc.date.available | 2015-07-28T06:09:14Z | |
| dc.date.issued | 1989-09 | |
| dc.description.abstract | Purification of cathepsin Β from buffalo-spleen, a hitherto unstudied system has been achieved by a simple procedure developed by incorporating suitable modifications in the existing methods for isolation of the enzyme from other sources. The purified enzyme has a molecular weight of 25 KDa and its Stokes radius was found to be 2·24 nm. Effects of several reducing agents, urea and thiol-protease inhibitors such as leupeptin and antipain, have been studied and the data unequivocally support the contention that the buffaloenzyme is similar to cathepsin Β from other tissues with respect to these properties. | en_US |
| dc.identifier.citation | Ahmad Sarfraz, Agarwal Sudhir K, Khan M Yahiya. Transplantation of fetal neocortex in rhesus monkey. Journal of Biosciences. 1989 Sep; 14(3): 261-268. | en_US |
| dc.identifier.uri | https://imsear.searo.who.int/handle/123456789/160737 | |
| dc.language.iso | en | en_US |
| dc.source.uri | https://www.ias.ac.in/jarch/jbiosci/14/261-268.pdf | en_US |
| dc.subject | Lysosomal proteases | en_US |
| dc.subject | cathepsin Β | en_US |
| dc.subject | buffalo-spleen | en_US |
| dc.subject | hydrodynamic properties | en_US |
| dc.title | Purification and some properties of buffalo spleen cathepsin Β. | en_US |
| dc.type | Article | en_US |