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NORMAN ALLEN, MD; ELIZABETH REAGAN, BA

Arch Neurol. 1964;11(2):144-154.

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

Introduction

β-Glucuronidase is a widely distributed enzyme which acts in acid pH optimum to hydrolyze the β-glycosidic bond between glucuronic acid and a variety of other moieties, including steroids, many hydroxylated aromatic compounds, and sugar derivatives. Its activities are particularly high in reproductive organs,¹ circulating leukocytes,^2,3 and activated macrophages⁴ as well as in epithelial tissues in general. Proposed natural substrates include the glucuronide conjugates of estrogens and other steroidal hormones and the oligosaccharide products of mucopolysaccharide degradation.¹ In most tissues, the enzyme exists predominantly in a latent form, distributing with lysosomes and microsomes.⁵ From this bound state, it may be released into a free or non-sedimentable form during the process of autolysis,⁶ ischemic necrosis,⁷ bacterial or traumatic shock,⁸ experimental muscular dystrophy,⁹ and vitamin A intoxication.¹⁰ In relation to the neoplastic process, most, but not all, human and experimental tumors show . . . [Full Text PDF of this Article]

Author Affiliations
CHAPEL HILL, NC

From the departments of Medicine (Neurology), Anatomy, and Biochemistry of the School of Medicine, University of North Carolina.

Footnotes
Submitted for publication Feb 3, 1964; accepted March 28.

Research Career Development Awardee of the National Institute of Health (Dr. Allen).

This work supported by grant CA-06466-02 of the National Institute for Neurological Diseases and Blindness, National Institutes of Health and, in part, by the American Cancer Society Institutional grant IN-15C.

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