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Complexometric Analyses of Serum and Serum Ultrafiltrates

HARRIS L. SMITH, M.D.; ROBERT L. FISCHER, Ph.D.; JAMES N. ETTELDORF, M.D.

Am J Dis Child. 1962;103(6):771-776.

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

Human muscular dystrophy is a condition of unknown etiology which produces progressive and severe dysfunction of symmetrical groups of skeletal muscle. Although its clinical manifestations^1-3 and patterns of heredity^4-6 have long been recognized, relatively little attention has been given the study of distribution and utilization of metal ions in this disorder. In recent years, new impetus has been given the study of metal ions in health and disease by the increasing recognition of their important influences upon activities of enzymes. In muscular dystrophy, abnormal activities of various glycogenolytic enzymes,^7-9 transaminase,¹⁰ nucleotidase,¹¹ and creatine phosphokinase¹² have been described. It is well known that all of the enzymes which catalyze the transfer of phosphate from adenosine triphosphate (ATP) to a phosphate receptor, or from a phosphorylated compound to adenosine diphosphate, (ADP) are activated by magnesium. Since ATP is necessary in such diverse functions as muscle contraction; . . . [Full Text PDF of this Article]

Author Affiliations

From the Pediatric Research Laboratory, Division of Pediatrics, College of Medicine, University of Tennessee, Memphis, and the Frank T. Tobey Memorial Children's Hospital, City of Memphis Hospitals, and the Le Bonheur Children's Hospital.; James N. Etteldorf, M.D., Frank T. Tobey Memorial Children's Hospital, 860 Madison Ave., Memphis 3.

Footnotes

This investigation was supported in part by a grant-in-aid from the Muscular Dystrophy Associations of America, Incorporated.

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