Electrophoretic separation of reptilian skeletal and cardiac muscle myosin heavy chain isoforms: Dependence on gel format

被引:2
|
作者
Reiser, Peter J. [1 ]
Bicer, Sabahattin [1 ]
机构
[1] Ohio State Univ, Div Biosci, Coll Dent, Columbus, OH 43210 USA
基金
美国国家科学基金会;
关键词
Electrophoretic mobility; Glycerol; Isoform; Myosin; Reptile; TRACHEMYS SCRIPTA-ELEGANS; FIBER-TYPE COMPOSITION; SHORTENING VELOCITY; RESOLUTION; CHAMELEONS; HINDLIMB; PROTOCOL; TURTLE; LIZARD;
D O I
10.1002/elps.201400221
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
This report provides a comparison of multiple gel formats to study myosin heavy chain (MHC) isoforms that are expressed in reptilian skeletal and cardiac muscles of five turtle species, water monitor, and prehensile tailed skink. Three gel formats were tested. The results identify one format that is superior, for the overall extent of electrophoretic separation and for the assessment of the number of MHC isoforms in reptilian striated muscles. The same format was shown previously to separate MHC isoforms that are expressed in American alligator. The results also show that another gel format reveals the distinct electrophoretic mobility of MHC isoforms in atrial, ventricular, and jaw adductor samples, compared to those expressed in skeletal muscles in the limbs and elsewhere in the body. In addition, the results reveal that the electrophoretic mobility of specific MHC isoforms, relative to other isoforms, depends on the gel format, as shown previously for mammalian and avian species. The discovery of the expression of masticatory MHC, which is abundantly expressed in jaw adductors of members of Carnivora and several other vertebrate orders, in the homologous muscles of prehensile tailed skink, an herbivore, and the carnivorous water monitor, was made during the course of this study.
引用
收藏
页码:2615 / 2620
页数:6
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