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Muscle proteins of the coelacanth Latimeria chalumnae Smith
Hamoir, G.; Piront, A.; Gerday, C.; Dando, P.R. (1973). Muscle proteins of the coelacanth Latimeria chalumnae Smith. J. Mar. Biol. Ass. U.K. 53(4): 763-784. hdl.handle.net/10.1017/S0025315400022463
In: Journal of the Marine Biological Association of the United Kingdom. Cambridge University Press/Marine Biological Association of the United Kingdom: Cambridge. ISSN 0025-3154, more
Peer reviewed article  

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Keyword
    Marine

Authors  Top 
  • Hamoir, G.
  • Piront, A.
  • Gerday, C., more
  • Dando, P.R.

Abstract
    Although the anatomy of the coelacanth muscles has been examined very thoroughly, their protein composition has, until recently, not been investigated. Thanks, however, to the 1972 British–French–American expedition to the Comores, frozen material has been made available and some results on myoglobin and four glycolytic enzymes have already been published. We have carried out a comparison of the sarcoplasmic proteins of red and white muscle by starch-gel electrophoresis. The ninhydrin-positive dialysable constituents and the myofibrillar proteins of white muscle have also been examined.A few puzzling results obtained with the white muscle extracts have been related to the occurrence of o.1 M ammonia, due presumably to the splitting of urea by a bacterial urease, and to an alteration of the active thiol groups of GAPDH and PK. If due account is taken of these unusual post-mortem changes, the extractability of the proteins and their properties are strikingly similar to those of teleosteans. The comparison of the sarcoplasmic proteins of white and red muscle by starch-gel electrophoresis revealed also that the differentiation observed in the coelacanth was similar to that occurring in the carp. A study of the low-molecular-weight proteins, or parvalbumins, of white muscle and of the myofibrillar proteins also shows the expected differences between the two muscle types.The only abnormal features observed in this study were the high concentration of parvalbumins, 1.5–2 times that found in other species examined, and the occurrence of an unusual globulin fraction which was easily extracted at ionic strength 0.5 and insoluble at ionic strength 0.35 and neutral pH.

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