An electrophoretic study of the low-molecular-weight components of myosin.
W. T. Perrie,S. V. Perry +1 more
TLDR
It is suggested that the Differences in the low-molecular-weight components of myosin from different types of muscle are a consequence of differences in the isoenzyme composition of the myosins.Abstract:
1. The low-molecular-weight components of myosin freshly prepared by the standard procedure from adult rabbit skeletal muscle migrated as four main bands Ml1, Ml2, Ml3 and Ml4 on polyacrylamide-gel electrophoresis in 8m-urea. 2. The number of bands increased on storage. This change was accelerated by increasing the temperature and pH. 3. None of the bands had electrophoretic mobilities identical with those of the well-characterized proteins of the myofibril or with the sarcoplasmic proteins. 4. By varying the ionic conditions and concentration of muscle mince used for the initial extraction it was possible to change the relative proportions of the two electrophoretic bands of intermediate mobility, Ml2 and Ml3. 5. The four-band picture similar to that obtained with rabbit was observed with myosin isolated from skeletal muscle of the rat, mouse, hamster, pigeon and chicken. 6. Rabbit cardiac myosin gave only two bands on electrophoresis. Myosin from rabbit red muscle gave a pattern intermediate between cardiac and white-skeletal-muscle myosin, i.e. the two fastest bands were present in decreased relative amounts. 7. It is suggested that the differences in the low-molecular-weight components of myosin from different types of muscle are a consequence of differences in the isoenzyme composition of the myosins.read more
Citations
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Journal ArticleDOI
Isoquinolinesulfonamides, novel and potent inhibitors of cyclic nucleotide dependent protein kinase and protein kinase C.
TL;DR: Both the holoenzyme and the catalytic subunit (or fragment), which is active without an enzyme activator, are susceptible to these compounds with a similar concentration dependency, thereby indicating that the inhibitory effect is attributed to the direct interaction of the compound with the active center of the enzyme but not with the enzymeactivator.
Journal ArticleDOI
Dynamic properties of mammalian skeletal muscles.
TL;DR: The author examines the relationship between ATPase activity of myosin and intrinsic speed of shortening, and the effects of nerve cross-union on properties of myOSin.
Journal ArticleDOI
Inhibition of forskolin-induced neurite outgrowth and protein phosphorylation by a newly synthesized selective inhibitor of cyclic AMP-dependent protein kinase, N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide (H-89), of PC12D pheochromocytoma cells.
Takashi Chijiwa,Atsushi Mishima,Masatoshi Hagiwara,Mamoru Sano,Kyozo Hayashi,Tsutomu Inoue,Naito Kenji,Tadashi Toshioka,Hiroyoshi Hidaka +8 more
TL;DR: In this article, a newly synthesized isoquinolinesulfonamide, H-89 (N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinoline-sulfoneamide), was shown to have a potent and selective inhibitory action against cyclic AMP-dependent protein kinase (protein kinase A), with an inhibition constant of 0.048 +/- 0.008 microM.
Journal ArticleDOI
Selective inhibition of catalytic activity of smooth muscle myosin light chain kinase.
TL;DR: Findings suggest that the ATP-binding site at the active center of smooth muscle myosin light chain kinase is located in a hydrophobic environment.
Journal ArticleDOI
Purification and characterization of smooth muscle myosin light chain kinase.
R.S. Adelstein,C.B. Klee +1 more
TL;DR: The enzyme phosphorylates the 20,000-dalton light chain of smooth muscle myosin more rapidly than the equivalent light chain from cardiac and skeletal muscles and does not phosphorylate histones, alpha-casein, phosphoryLase kinase, orosphorylase b at a significant rate.
References
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The relaxing protein system of striated muscle. Resolution of the troponin complex into inhibitory and calcium ion-sensitizing factors and their relationship to tropomyosin
M. C. Schaub,S. V. Perry +1 more
TL;DR: Evidence is presented indicating that the ability of tropomyosin preparations to restore relaxing-protein-system activity to the troponin complex and their inhibitory effect on the Ca(2+)-stimulated adenosine triphosphatase activity of desensitized actomyOSin are two properties of different stability to preparative procedures and tryptic digestion.
Journal ArticleDOI
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TL;DR: Ammonium persulfate, a common polymerizing agent for acrylamide gels, can inactivate yeast enolase and produce increased electrophoretic heterogeneity during disc electrophoresis in gels containing 8M urea.
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