A study of the phenomena and causation of heat-contraction of skeletal muscle / by T.G. Brodie and S.W.F. Richardson ; communicated by W.D. Halliburton.
- Brodie, Thomas Gregor, 1866-1916.
- Date:
- 1899
Licence: Public Domain Mark
Credit: A study of the phenomena and causation of heat-contraction of skeletal muscle / by T.G. Brodie and S.W.F. Richardson ; communicated by W.D. Halliburton. Source: Wellcome Collection.
Provider: This material has been provided by The University of Glasgow Library. The original may be consulted at The University of Glasgow Library.
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![time; but that the action of a temperature of 40° C. for a few seconds produces practically the same result as a stay of some minutes at a lower temperature. (It is important to note in this connection that, by the method Gotschlich uses, in order to expose a muscle to a temperature of 40° C. the rise must he gradual, for the muscle is suspended in air.) 9. He ultimately concludes'^ that this condition is of the same nature as heat-rigor, i.e., it is qualitatively an incomplete rigor, and that the processes underlying the two conditions are chemical in nature, the one being an earlier phase of the other. Before we proceed to a discussion of the results we have obtained, it will be convenient to consider the different proteids obtainable from muscle, for their temperatures of coagulation play an important part in the interpretation we place upon our results. Our knowledge is chiefly derived from the experiments of KuhneI and Halliburton,! which have recently been extended and modified in many important particulars by v. Furth.§ These proteids, for the case of frog muscle, may he arranged in a series as follows :— (1.) An albumin (myo-alhumin of Halliburton), which coagulates at 73° C. This is only present in small quantities, and by v. Furth is considered as an impurity due to admixture with a little blood-serum or lymph, (2.) Myoglobulin (Halliburton). This again is only present in small quantities, v, Furth considers that it is in reality a small quantity of the next proteid remaining in solution after most has been precipitated. (3.) Myosinogen (Halliburton), or myogen (v. Furth). This is the most important proteid. It is chiefly coagulated at a temperature of 56° C. The limits given by v. Furth || for the coagulation temperature of a salt-free solution are from 55° to 65° C., with a maximum precipitation at about 58° C. Weak solutions require a rather higher temperature. (4.) Paramyosinogen (Halliburton), musculin (Hammarsten), or myosin (Kuhne and v. Forth). Forms a high proportion of the total proteid and coagulates at about 47° C, The temperature limits found by v. FurthIT are, from 44° to 47° C. an opalescence and clouding, and a precipitate from 47° to 50° C. (5.) Soluble myogen-flbrin (v. Furth). This proteid is present in considerable quantities in frog’s muscle-plasma. Its solutions begin to cloud when a temperature of 30° C. is reached, and give a coagulum between 32° and 40° C. Loc. cit., pp. 154, 155. t ‘ Myologische Untersuchungen,’ 1860. ‘Ueber das Protaplasma und die Contractilitat,’ Leipzig^ 1864. Muller’s‘Archiv,’1859. t ‘ Journ. of Physiol,’ vol. 8, p. 133, 1887. § ‘Arch. f. exp. Path. u. Pharm.,’ vol. 36, p. 231, 1895. 1] Loc. cit., p. 243. •II Loc. cit., p, 238.](https://iiif.wellcomecollection.org/image/b24917230_0014.jp2/full/800%2C/0/default.jpg)
