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PURIFICATION AND QUANTITATION OF GLUTARALDEHYDE AND ITS EFFECT ON SEVERAL ENZYME ACTIVITIES IN SKELETAL MUSCLE

PAUL J. ANDERSON 1

1 Department of Neuropathology, Mount Sinai School of Medicine, New York, New York

Glutaraldehyde was quantitated by chemical titration, osmometry and ultraviolet spectrophotometry. Pure glutaraldehyde exhibited an absorption maximum at 280 mµ and absorbance at this wavelength conformed to Beer's law. A second maximum at 235 mµ indicated the presence of "impurities" (probably of polymeric origin), and effective purification was achieved by distillation or by repeated washing with charcoal of high surface area (Norit EX). Purified glutaraldehyde was stable when stored under nitrogen or freon at 4°C. Representative oxidoreductase, transferase and hydrolase activities were measured in supernatants and sediments of skeletal muscle homogenates that had been treated with glutaraldehyde samples of low, intermediate and high impurity content (based on relative absorbance at 235 mµ). Enzyme recovery was inversely related to impurity content, the highest levels being obtained from tissue treated with the purest glutaraldehyde.

Submitted on June 26, 1967


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 Journal of Bioactive and Compatible PolymersHome page
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Chemical Modifications of Heparin.1: Reaction of Partially N-Desulfated Heparin with Glutaraldehyde
Journal of Bioactive and Compatible Polymers, January 1, 1994; 9(3): 267 - 281.
[Abstract] [PDF]



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