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H Spadiut

Publications and source records attributed to H Spadiut.

7 recordsLinked to original sources

[Enzyme histochemical studies on the epithelium of the epididymis of the tomcat (author's transl)].

The histochemical localization of some oxidoreductases was investigated in the epididymides of adult tomcats. Succinate dehydrogenase, lactate dehydrogenase, beta-hydroxybutyrate-dehydrogenase revealed their highest activity in corpus and cauda epididymidis whereas glucose-6-phosphate-dehydrogenase was strongest in the caput. The activity of the diaphorases and of cytochrome oxidase in the epididymal epithelium increased from caput towards the cauda epididymidis. The reaction for isocitrate dehydrogenase was distinct throughout the whole length of the ductus epididymidis. Our findings were compared with the biochemical results of other authors and the functions of the oxidoreductases in the epididymal epithelium were briefly discussed.

Animals

[Histotopics of lysosomal enzymes in the epididymis of the tom-cat (author's transl)].

The histochemical localization of 6 lysosomal enzymes was studied in the epididymis of adult tomcats. A weak to distinct reaction for acid phosphatase, leucyl-amino-peptidase and non--specific esterase could be observed in the epithelium of the ductus epididymidis in all three segments. Among the glycosidases, N-acetyl-beta-glucosaminidase displayed the strongest activity. alpha-man and alpha-fuc could not be demonstrated. For N-Acetyl-beta-glucosaminidase, beta-Galactosidase, acid phosphatase and non-specific esterase, an increase of enzyme activity from the initial segment towards the terminal segment was seen. Intracellularly, the maximum of enzyme activity of those four enzymes was supranuclear. This histochemically enstablished pattern of enzyme activity in the epididymis of the tomcat was compared with those of other mammals. The possible functions of enzymes in the epididymis was briefly discussed.

Acid Phosphatase