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II. Pulmonary Embolism, Liver Disease, the Postoperative State, and Other Medical Conditions

Nelson P. Trujillo, MD; Donald Nutter, MD; John M. Evans, MD

Arch Intern Med. 1967;119(4):333-344.

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

The DETERMINATION of serum lactic dehydrogenase (LDH) activity is used in the diagnosis of a wide variety of conditions such as myocardial infarction,¹ pulmonary embolism,² hepatobiliary diseases,³ musculoskeletal disorders,⁴ certain neoplasms,⁵ and a variety of hematological diseases.⁶ Hence, to a considerable degree, this enzyme lacks specificity as a diagnostic aid. The separation of LDH into its component isoenzymes represents an attempt to improve its specificity.

Lactic dehydrogenase in man consists of five heterogenous isoenzymes. Lactic dehydrogenase 1, the electrophoretically slowest isoenzyme, is present in largest concentration in liver and skeletal muscle, while LDH 5, the electrophoretically fastest isoenzyme, is found in largest concentration in heart muscle and erythrocytes. Lactic dehydrogenase 2, 3, and 4 are distributed widely and in varying amounts in reticuloendothelial, lung, heart, and other tissues.⁷ It has been assumed that serum LDH isoenzyme activity in disease states reflects, at least in part, the isoenzyme activity of tissue . . . [Full Text PDF of this Article]

Author Affiliations
Washington. DC

From the Department of Medicine, George Washington University Hospital, and the School of Medicine, George Washington University, Washington, DC.

Footnotes
Received for publication Sept 12, 1966; accepted, Dec 15.

Reprint requests to George Washington University Hospital, 901 23rd St NW, Washington, DC 20037 (Dr. Evans).

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