Quantification of carbonic anhydrase III and myoglobin in different fiber types of human psoas muscle.
Carbonic anhydrase (CA III) and myoglobin contents from isolated human muscle fibers were quantified using a sensitive time-resolved fluoroimmunoassay. Human psoas muscle specimens were freeze-dried, and single fibers were dissected out and classified into type I, IIA and IIB by myosin ATPase staining. Fiber typing was further confirmed by SDS-PAGE. CA III and myoglobin were found in all fiber types. Type I fibers contained higher concentrations of CA III and myoglobin than type IIA and IIB fibers. The relative concentrations of CA III in type IIA and IIB fibers were respectively 24% and 10% of that in type I fibers. The relative concentrations of myoglobin in type IIA and IIB fibers were 60% and 28% of that in type I fibers. Anti-CA III immunoblotting results from fiber-specific pooled samples agreed well with quantitative measurements. The results indicate that CA III is a more specific marker than myoglobin for type I fibers.
Zheng
A
A
Department of Anatomy, University of Oulu, Finland.
Rahkila
P
P
Vuori
J
J
Rasi
S
S
Takala
T
T
Väänänen
H K
HK
D002256:Carbonic Anhydrases / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D005455:Fluorescent Antibody Technique; D006801:Humans; D015151:Immunoblotting; D009132:Muscles / Q000166:cytology / Q000201:enzymology / Q000378:metabolism*; D009211:Myoglobin / Q000032:analysis*; D009218:Myosins / Q000378:metabolism
D009211:Myoglobin; D009218:Myosins; D002256:Carbonic Anhydrases