Histochemical and biochemical studies of the hepatopancreas peroxidase of the freshwater crayfish, Cambarus robustus

Document Type

Article

Publication Date

1-1-1985

Abstract

Crayfish are among the few invertebrate species reported to possess endogenous peroxidase activity. The enzyme is found within the hepatopancreas, the principal digestive and absorptive organ of the crustacean body. Cambarus robustus, a species found in abundance in the streams of western New York, was used in this study. Homogenates of 18 hepatopancreases were assayed for peroxidase activity using guaiacol as the substrate. Although present in all organs, peroxidase activity displayed a greater than 50‐fold difference between the two extremes (0.05–;2.72 units/mg protein). Histochemical examination using diaminobenzidine revealed peroxidase activity within a line of cells extending along the distal two‐thirds of the lengths of all hepatopancreatic tubules. The cells function to synthesize the enzyme, sequester it within vacuoles of increasing size, and eventually secrete it into the tubule lumen. Since the tubule is constantly renewed by distal mitotic activity and concomitant proximal exfoliation, this histochemical technique permits not only the examination of the ontogeny of this peroxidase‐positive cell line, but also offers additional insight into the mechanism of hepatopancreatic tubule renewal. Copyright © 1985 Wiley‐Liss, Inc.

Publication Source (Journal or Book title)

Journal of Morphology

First Page

171

Last Page

182

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