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ALAN E. H. EMERY, MSc, MB, ChB, PhD; DONALD H. SHERBOURNE, BSc, MB, BS; ALLEN PUSCH, MD

Arch Neurol. 1965;12(3):251-257.

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Introduction

THE ELECTROPHORETIC pattern of the enzyme lactic dehydrogenase (LDH) is composed of several bands which are believed to be different molecular forms of the enzyme and have been called "isozymes."¹⁷ It has been suggested that these isozymes result from various tetrameric associations of two subunits referred to as A and B by Markert,^1,15 and as M and H by Cahn et al.⁴ Experimental evidence supporting this idea has been presented recently.¹⁶

The electrophoretic pattern of LDH isozymes is tissue specific. Wróblewski and Gregory²³ showed that of all the different tissues they examined no two appeared to have exactly the same LDH pattern. The LDH isozyme pattern of human skeletal muscle is composed of five bands. The cathodic or most slowly migrating band (LDH-5) predominates whereas the anodic or most rapidly migrating bands (LDH-1 and LDH-2) are reduced. Dreyfus et al⁹ and Wieme . . . [Full Text PDF of this Article]

Author Affiliations
BALTIMORE

From the Division of Medical Genetics (Dr. Emery), the Department of Medicine (Dr. Sherbourne), and the Department of Pathology (Dr. Pusch) of the Johns Hopkins University School of Medicine.

Footnotes
Submitted for publication Sept 11, 1964; accepted Nov 3.

Reprint requests to Division of Medical Genetics, Manchester University Department of Medicine, Manchester, England (Dr. Emery).

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