Quantitative studies on the structure of cross-striated myofibrils. II. Investigations by biochemical techniques |
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| Authors: | HANSON J HUXLEY H E |
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| Affiliation: | 1. College of Animal Science and Technology, Henan Agricultural University, Zhengzhou 450002, China;2. Henan Key Laboratory for Innovation and Utilization of Chicken Germplasm Resources, Zhengzhou 450046, China;3. International Joint Research Laboratory for Poultry Breeding of Henan, Zhengzhou 450002, China;1. Laboratory of Muscular Biopathology, Department of Comparative Anatomy and Pathological Anatomy, Faculty of Veterinary Sciences, University of Cordoba, Campus Universitario de Rabanales, 14014 Cordoba, Spain;2. Animal Genomics Laboratory, School of Agriculture and Food Science, College of Agriculture, Food Science and Veterinary Medicine, University College Dublin, Belfield, Dublin, Ireland;1. Department of Large Animal Clinical Sciences, College of Veterinary Medicine, Michigan State University, East Lansing MI;2. Department of Clinical Sciences, Carlson College of Veterinary Medicine, Oregon State University 227 Magruder Hall, OR |
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| Abstract: | The quantities of various protein fractions in the psoas muscle of the rabbit have been determined by chemical analysis.The soluble protein removed by glycerol extraction and by the subsequent isolation and washing of the fibrils in neutral hypotonic salt solution, make up 34% of the total protein of the whole muscle.62% of the total protein of the washed fibrils is taken out by myosin-extracting procedures.82% of the extracted protein precipitates when the ionic strength is reduced to 0.04; this component is conventionally known as myosin. Thus the myosin extracted makes up 51% of the total protein of the washed fibrils, and the removal of the myosin is accompanied by the extraction of a further 11% of the total protein.In the accompanying paper5 it has been shown by interference microscopy that the quantity of A substance in similar fibrils is 50–55% of their total protein, and that the same myosin-extracting procedures remove the A substance and another 10% of the total protein, 60–65% in all.These comparative measurements by interference microscopy and chemical analysis prove that at least four-fifths of the myosin in these fibrils is present as the A substance, and the results are in excellent agreement with the hypothesis that all the myosin is concentrated in the A bands. |
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