The general structure of the myosin filament has been known since the classical x-ray diffraction studies of Huxley and Brown (1963). However, one of the crucial features, namely, the filament ordering or the number of myosin cross-bridges per 143 Å repeat, has been controversial throughout (Squire, 1981). Analysis of myofibrillar proteins by means of one-dimensional sodium dodecyl sulfate polyacrylamide gels has yielded conflicting results. This author reinvestigated the myosin to actin stoichiometry from one-dimensional gels of myofibrils prepared by different procedures. Next, this author addressed the critical issue of whether the differences in actin concentration during the different methods of muscle preparation were a result from loss of actin or removal of contaminants that comigrate with actin. In examining this question, two-dimensional electrophoresis, sodium dodecyl sulfate in the first dimension and isoelectric focusing in the second dimension were performed on myofibrillar preparations of rabbit muscle. Results revealed a structural arrangement of myosin cross-bridges in vertebrate striated muscle.
| Autorius: | Pat Precin |
| Leidėjas: | LAP LAMBERT Academic Publishing |
| Išleidimo metai: | 2016 |
| Knygos puslapių skaičius: | 80 |
| ISBN-10: | 3659890960 |
| ISBN-13: | 9783659890963 |
| Formatas: | 220 x 150 x 5 mm. Knyga minkštu viršeliu |
| Kalba: | Anglų |
Parašykite atsiliepimą apie „Structural Arrangement of Myosin: Evidence for Cross-Bridge Arrangement in Vertebrate Striated Muscle“
