NATURE OF LYSOSOMAL ANGIOTENSINASE ACTIVITY

スポンサーリンク

概要

• 論文の詳細を見る

• Acid angiotensinase activity is present in lysosomes of rat kidney and liver. The nature of this activity was investigated by bioassay and paper chromatography, using various angiotensin analogues as substrates. The main part of the lysosomal angiotensinase activity, especially on [Ile^5]-angiotensin II, is due to a carboxypeptidase which releases C-terminal phenylalanine. This enzyme is independent of sulthydryl groups and is inhibited by DFP. It is differentiated from cathepsin A or catheptic carboxypeptidase by its heat stability. The remaining part of the angiotensinase activity is sulthydryl-dependent and not inhibited by DFP. This is attributed to a chymotrypsin-like or a trypsin-like action or both. Rat plasma after dialysis against EDTA had a slight acid angiotensinase activity and released phenylalanine.

• 社団法人日本循環器学会の論文
• 1971-04-20

著者

• Matsunaga Masao

  The Third Diviston Of Internal Medicine School Of Medicine. Kyoto University

• Matsunaga Masato

  The Third Diviston of Internal Medicine, School of Medicine. Kyoto University

関連論文

• NATURE OF LYSOSOMAL ANGIOTENSINASE ACTIVITY

スポンサーリンク