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Eduardo Bonilla, MD; Donald L. Schotland, MD

Arch Neurol. 1970;22(1):8-12.

	Since this article does not have an abstract, we have provided the first 150 words of the full text PDF and any section headings.

MUSCLE phosphofructokinase (PFK) deficiency in man was first described by Tauri et al¹ in a biochemical investigation in 1965. In 1967, Layzer et al² reported additional biochemical and immunologic studies in a second family with this disease. This disorder may be regarded as a fourth type of muscle glycogenosis³ in addition to deficiencies of phosphorylase, amylo-1,6-glucosidase (debrancher) and amylo-1,4-glucosidase (acid maltase).

The PFK catalyzes the conversion of fructose-6-phosphate (F-6-P) to fructose-1,6-diphosphate (F-1,6-PP); in the absence of this enzyme, glycogen cannot be broken down to lactic acid (Fig 1). The clinical features of this disease are identical to muscle phosphorylase deficiency (McArdle's disease) and include muscle cramps, exercise intolerance, contracture following ischemic work, and myoglobinuria.⁴

At the present time, phosphorylase deficiency can be detected by histochemical means prior to biochemical studies,^5,11 but a histochemical method for the detection of muscle PFK deficiency is not . . . [Full Text PDF of this Article]

Author Affiliations
Philadelphia

From the Neurological Clinical Research Center and the Spiller Neurological Unit, University of Pennsylvania Hospital, Philadelphia.

Footnotes
Submitted for publication July 5, 1969; accepted July 21.

Reprint requests to Spiller Neurological Unit, University of Pennsylvania Hospital, Philadelphia 19104 (Dr. Schotland).

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