Trypsin digestion of arginase: evidence for a stable conformation manganese directed.
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.
Díez
A M
AM
Departamento de Bioquímica y Biología Molecular y Genética, Universidad de Extremadura, Facultad de Veterinaria, Cáceres, Spain.
Campo
M L
ML
Soler
G
G
D000818:Animals; D001119:Arginase / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D004795:Enzyme Stability; D066298:In Vitro Techniques; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D008345:Manganese / Q000378:metabolism / Q000494:pharmacology; D011487:Protein Conformation / Q000187:drug effects; D051381:Rats; D014357:Trypsin / Q000494:pharmacology
D008345:Manganese; D014357:Trypsin; D001119:Arginase