Further observations on myohaematin and the histohaematins / by C.A. MacMunn.

  • MacMunn, Charles Alexander, 1852-1911.
Date:
[1887]
Catalogue details

Licence: Public Domain Mark

Credit: Further observations on myohaematin and the histohaematins / by C.A. MacMunn. Source: Wellcome Collection.

Provider: This material has been provided by The Royal College of Surgeons of England. The original may be consulted at The Royal College of Surgeons of England.

    5/20 (page 53)
    tions mentioned above showed only myohaematin bands, no haemoglobin, as shown in PI. II. sp. 3. Upon boiling such a solution the coagulum which forms no longer shows any distinct bands; this is in accordance with a former result, as I found that sufficient heat destroys the bands in muscle itself. Coagulation by means of absolute alcohol on the contrary allows the bands to be recognised in the yellowish coagulum, especially if it be treated with a reducing agent. In some filtrates obtained from salted muscle, the band before D was missing, sp. 4 being seen instead. The faint band after D did not disappear with ammonium sulphide, showing that it did not belong to haemoglobin. In some cases the coagulum, produced by adding alcohol to the filtrate from salted muscle, when extracted with rectified spirit and caustic potash showed a band like that of alkaline haematin at D, sp. 5; but it is worthy of notice, although I do not attach much importance to this result for reasons to be mentioned again, that this band did not go with ammonium sulphide, while another faint band betweeu D and E appeared, this latter however is not the dominant reduced myohaematin baud as it is nearer the red than the latter. Such coagula were extracted by various solvents including glycerine and water with a negative result, the colouring matter clinging most tenaciously to the coagulated proteid. Several proteids appear to be present in the filtrate from salted muscle, and all the myohaematin is not carried down completely until the solution has been heated sufficiently to carry down the last proteid. When the filtrate from salted muscle is concentrated in vacuo over sulphuric acid, it becomes redder and the bands can be seen very distinctly, they read after concentration as follows:—■ 1st, \ 589 to X 571, 2nd, \ 5535 to \ 545, 3rd, uncertain (see sp. 7). But it is quite evident that the myohaematin here is not the same as it exists in muscle, the bands being those of modified myohaematin. The first band of sp. 7 does not belong to oxyhaemoglobin as it persists after the use of sulphide of ammonium. Probably during the extraction of the myosin and during the subsequent concentration in vacuo, changes take place which account for the change of spectrum. I succeeded in procuring haematoporphyrin by acting with sulphuric acid on the coagulum produced by absolute alcohol on the filtrate of salted muscle, and filtering through asbestos, but owing to the doubt which I felt 5—2