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Creatine kinase, a histochemical study by the gelatin film-lead precipitation technique

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Summary

A modification of the method of Hori (1966) has permitted the precise histochemical localization of a portion of the creatine kinase activity in muscle. ATP produced by the action of this enzyme is hydrolysed by adjacent ATPase to inorganic phosphate. This is precipitated as lead phosphate, and then visualised by conversion to brown lead sulphide. The application of the incubation medium in the form of a viscous gelatin film has permitted localization of the lead sulphide in a clearly defined net-like pattern throughout the sarcoplasm. The results of this study are discussed in terms of the role of creatine kinase in the sarcoplasmic reticulum.

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Khan, M.A., Holt, P.G., Papadimitriou, J.M. et al. Creatine kinase, a histochemical study by the gelatin film-lead precipitation technique. Histochemie 32, 49–58 (1972). https://doi.org/10.1007/BF00277470

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