Trypsin digestion of arginase: evidence for a stable conformation manganese directed. |
| |
Authors: | A M Díez M L Campo G Soler |
| |
Affiliation: | Departamento de Bioquímica y Biología Molecular y Genética, Universidad de Extremadura, Facultad de Veterinaria, Cáceres, Spain. |
| |
Abstract: | 1. Controlled tryptic digestion of native arginase from rat liver suggests that Mn2+ promotes a stable conformation as shown by the following features. 2. An 18-fold increase in the half-life of arginase activity in the presence of Mn2+ is produced. 3. The stability of subunit B of arginase is increased in the presence of Mn2+ as revealed by SDS-PAGE during the time-course of trypsin cleavage. 4. The different digestion products of arginase with and without Mn2+ appearing during the time-course of tryptic treatment. 5. Different activity/bands protein ratio at any time of the tryptic digestion in the incubation mixtures, with and without Mn2+, are apparent. |
| |
Keywords: | |
本文献已被 ScienceDirect 等数据库收录! |
|