2-D analysis of human skeletal muscle myosin light chains with immobilized pH gradients.
Myosin light chains (LC) are a low molecular mass fraction non-covalently bound to the heavy chains. They are present in the myosin molecules and exhibit various degrees of polymorphism among the different species. By utilizing a highly-resolving 2-D technique, in narrow immobilized pH gradients, we have compared the LC forms of skeletal muscle in human and rabbit. Our findings: (1) both forms, LC1 and LC3, migrate in the two species with rather similar electrophoretic constants (both in terms of pI and Mr); (2) the LC2 forms of rabbit and humans exhibit the same Mr but quite different pI values, the rabbit forms being more acidic; (3) the chain LC2Sb is resolved into two spots in both rabbit and humans. In the former, the two bands have equal intensity, while in the latter the high pI component is clearly the most abundant.
Pernelle
J J
JJ
Institut de Pathologie et Biologie Cellulaires et Moleculaires, U 15, Paris, France.
Righetti
P G
PG
Wahrmann
J P
JP
D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D015879:Myosin Subfragments; D009218:Myosins / Q000032:analysis*; D010446:Peptide Fragments / Q000032:analysis*; D010449:Peptide Mapping / Q000379:methods*; D011817:Rabbits
D015879:Myosin Subfragments; D010446:Peptide Fragments; D009218:Myosins