Substrate Specificity and Histochemical Distribution of Aminopeptidase in Rat Testis and Epididymis
スポンサーリンク
概要
- 論文の詳細を見る
The substrate specificity of rat testicular and epididymal peptidase was investigated using chromogenic substrates, D. L-alanine-, L-arginine-, γ-N-L-glutamine-, L-leucine-, D. L-methionine-, α-N-benzoyl-D. L-arginine-, and N-benzoyl-L-leucine-β-naphthylamide. The histochemical distribution of peptidase activity demonstrated with these substrates was also investigated in the testis and epididymis.<BR>L-Arginine-β-naphthylamide (Arg-β-NA) and γ-N-L-glutamine-β-naphthylamide (Glu-β-NA) were mostly hydrolyzed in the testis and epididymis, respectively.<BR>Histologically, the activity using Arg-β-NA as substrate (animopeptidase B) appeared in both the cytoplasms and nuclei of interstitial cells and spermatogonia and the heads of spermatozoa, while activity using other substrates was found only in the cytoplasms of cells in the germinal epithelium. In the epididymis, strong reaction with Glu-β-NA (γ-glutamyl transpepetidase) was found in the apical part of the epithelial cells and in the heads of spermatozoa.<BR>Neither α-N-benzoyl-L-arginine-nor N-benzoyl-L-leucine-β-naphthylamide was utilized in either the testis or the epididymis.
- 社団法人 日本内分泌学会の論文
著者
関連論文
- Electrophoretic and Histochemical Studies on Hepatic 3α-Hydroxysteroid Dehydrogenase in the Rat
- Substrate Specificity and Histochemical Distribution of Aminopeptidase in Rat Testis and Epididymis
- Staining Specificity of Histochemical Reaction for 3β-Hydroxysteroid Dehydrogenase Activity in Mouse Testis
- A Micromethod for Protein Assay Using a Light Microscope.