New Chromogenic Arginine Anilide Substrates for Trypsin and Thrombin
dc.contributor.author | Okiei, W.O. | |
dc.contributor.author | Somorin, O. | |
dc.date.accessioned | 2019-09-27T07:35:00Z | |
dc.date.available | 2019-09-27T07:35:00Z | |
dc.date.issued | 2003 | |
dc.description.abstract | Fifteen chromogenic anilide substrates, namely N-benzyloxycarbonyl-L-arginine-X-substituted anilides (X= H, F, Cl, Br, I, NO2, CF3, CH3 or OCH3) at the meta or para position of the aniline ring, were synthesized using the procedure earlier reported. These substrates are suitable for studying the electronic effects of substituents on trypsin as well as on thrombin hydrolytic activities. The hydrolysis of these substrates by trypsin or thrombin at 37oC and pH 8.4 was found to proceed at significantly different rates in the following order: L-ZAPA.HCl>L-ZAPT.HCl>L-ZAPIA.HCl>ZAPBA.HCl> L-ZAMT. HCL> L-ZAPNA.HCl>L-ZAPCA.HCl>L-ZAMA.HCl>ZAMNA.HCl> L-ZAMTHA. HCL>L ZAPFA.HCl>L-ZAMCA.HCl>L-ZAA.HCl>L-ZAMFA.HCl>L-ZAMTFA.HCl The Km values obtained for the thrombin-catalyzed hydrolysis of the arginine substrates were generally higher than those of the trypsin-catalyzed hydrolysis of the same anilides. | en_US |
dc.identifier.citation | Okiei, W., & Somorin, O. (2003). New Chromogenic Arginine Anilide Substrates for Trypsin and Thrombin. African Journal of Science, 35, 165-172. | en_US |
dc.identifier.uri | https://ir.unilag.edu.ng/handle/123456789/6196 | |
dc.language.iso | en | en_US |
dc.subject | Research Subject Categories::NATURAL SCIENCES::Chemistry | en_US |
dc.subject | anilide | en_US |
dc.subject | arginine | en_US |
dc.subject | chromogenic | en_US |
dc.subject | trypsin | en_US |
dc.subject | thrombin | en_US |
dc.title | New Chromogenic Arginine Anilide Substrates for Trypsin and Thrombin | en_US |
dc.type | Article | en_US |
Files
Original bundle
License bundle
1 - 1 of 1
Loading...
- Name:
- license.txt
- Size:
- 1.71 KB
- Format:
- Item-specific license agreed upon to submission
- Description: