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HISTOCHEMICAL DETECTION OF PHOSPHORYLASE IN ANIMAL TISSUES

Journal of Histochemistry & Cytochemistry · 1955 · Vol. 3(3) · pp. 153–160
Tadao TakeuchiHIDEO KURIAKI

Abstract

Amylophosphorylase in animal tissues has been demonstrated in frozen sections by use of activators and primer in a modified Yin and Sun method. A suitable technique for this purpose was newly devised. It was experimentally proved that the synthesis of glycogen from glucose-1-phosphate in tissues was specifically due to phosphorylase activity itself. Amylophosphorylase was histochemically demonstrated in muscle fibers of skeletal and heart muscles, smooth muscles in certain organs, epithelium of esophagus etc. The reactions were shown in cytoplasms and the nuclei were not stained. The phosphorylase reaction of muscle was very closely related to striated structure in muscle fibers.

Glycogen Storage Diseases and MyoclonusBone and Dental Protein StudiesMitochondrial Function and PathologyGlycogen phosphorylaseGlycogenChemistryEpitheliumFrozen section procedureSkeletal musclePrimer (cosmetics)BiochemistryAnatomyBiology

MeSH terms

AnimalsColoring AgentsPhosphorylasesHumansStaining and Labeling
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