Metallothionein isoforms from horse, rabbit and rat separated by capillary zone electrophoresis at low pH.
A comparative study of MT isoforms in rat liver and in commercial Sigma MT preparations from rabbit liver and horse kidney was performed using capillary zone electrophoresis (CZE). Electropherograms revealed the co-migration of MT forms from these species. A special form, the a-form (not binding Cd), occurred in various MT samples in different amounts, depending on the method used for MT purification. In the rabbit liver electropherogram a main form appeared (the b-form), which might be a modified MT form. A band of unknown composition, running ahead of the rat liver MT-I and -II forms on polyacrylamide gels, not having Cd binding affinity, probably had its counterpart in a yet unidentified CZE peak. CZE electropherograms of purified MT samples may contain main peaks that do not represent genuine and functional MT isoforms. Results are also presented which indicate that at low pH the MT-II form is more unstable than MT-I.
Wilhelmsen
T W
TW
Pharmaceutical Department, The Norwegian Medicines Control Authority, Sven Oftedalsvei 6, N-0950 Oslo, Norway.
Olsvik
P A
PA
Teigen
S W
SW
Andersen
R A
RA