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Structural Arrangement of Myosin: Evidence for Cross-Bridge Arrangement in Vertebrate Striated Muscle - Softcover
Inhaltsangabe
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.
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Reseña del editor
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.
Biografía del autor
Dr. Precin, PhD, PsyaD, NCPsyA, LP, OTR/L, FAOTA. MS Biophysics, Manhattan psychoanalyst, Faculty Touro College & NPAP, occupational therapist. Book publications: Relationship between Mentalization & Psychosomatic Illness, Living Skills Recovery Workbook, Client Centered Reasoning, Surviving 9/11, Healing 9/11, & Issues in Psychoanalysis.
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Structural Arrangement of Myosin
Verlag:
LAP LAMBERT Academic Publishing Mai 2016, 2016
ISBN 10: 3659890960
ISBN 13: 9783659890963
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Taschenbuch
Anbieter: buchversandmimpf2000, Emtmannsberg, BAYE, Deutschland
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Taschenbuch. Zustand: Neu. Neuware -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.Books on Demand GmbH, Überseering 33, 22297 Hamburg 80 pp. Englisch. Artikel-Nr. 9783659890963
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Structural Arrangement of Myosin: Evidence for Cross-Bridge Arrangement in Vertebrate Striated Muscle
Verlag:
LAP LAMBERT Academic Publishing, 2016
ISBN 10: 3659890960
ISBN 13: 9783659890963
Neu
Paperback
Anbieter: Revaluation Books, Exeter, Vereinigtes Königreich
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Paperback. Zustand: Brand New. 80 pages. 8.66x5.91x0.19 inches. In Stock. Artikel-Nr. 3659890960
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