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Research on molecular mechanisms ofMcArdle's disease (muscle glycogen phosphorylase deficiency)
Author(s) -
DAEGELENPROUX D.,
KAHN A.,
MARIE J.,
DREYFUS J.C.
Publication year - 1981
Publication title -
annals of human genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.537
H-Index - 77
eISSN - 1469-1809
pISSN - 0003-4800
DOI - 10.1111/j.1469-1809.1981.tb00312.x
Subject(s) - glycogen phosphorylase , glycogen storage disease , enzyme , glycogen , biochemistry , phosphorylase kinase , glycogen debranching enzyme , biology , chemistry
SUMMARY McArdle'@ disease is due to the lack of activity of muscle glycogen phosphorylase. We investigated the presence of an inactive protein by two techniques: ( a ) tridimensional protein maps, using a modification of the originalO'Farrell technique allowing location of phosphorylase. ( b ) Purification of enzyme from crude muscle extracts, using an immunoaffinity micro‐chromatographic procedure. Protein maps of three patients were obtained. No protein was detected at the normal (97 K) position of phosphorylase but 70 and 60 K spots were visible. Results of enzyme purification by immunoaffinity were negative for one patient, whereas a small band of phosphorylase‐like material was detected in the other. Our results confirm the molecular heterogeneity of the disease. We think such methods might be useful for investigating other genetic diseases.