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Planta Med 1987; 53(1): 19-21
DOI: 10.1055/s-2006-962608
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© Georg Thieme Verlag Stuttgart · New York

Bradykinin-Degrading Glycoprotein in Aloe arborescens var. natalensis

Akira Yagi1 , Nobuo Harada2 , Koichiro Shimomura3 , Itsuo Nishioka4
  • 1Faculty of Pharmacy and Pharmaceutical Sciences, Fukuyama University, Fukuyama, Hiroshima, 729-02, Japan.
  • 2Banyu Pharmaceutical Co. Ltd., Nihonbashi-honcho, Chuo-ku, Tokyo 103, Japan.
  • 3Tsukuba Experimental Station of Medicinal Plants, National Institute of Hygenic Sciences, Yatabe-cho, Tsukuba-gun, Ibaraki, Japan.
  • 4Faculty of Pharmaceutical Sciences, Kyushu University, Fukuoka 182, Japan.
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Publication History

1986

Publication Date:
24 January 2007 (online)

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Abstract

A homogeneous glycoprotein (aloe glycoprotein; mol. mass 40,000) containing 50.7% of protein was isolated from an extract of A. arborescens var. natalensis by precipitation with 60% ammonium sulfate. Aloe glycoprotein had bradykinin-degrading activity on an isolated guinea pig ileum in vitro. Peptide analyses using a reversed-phase, high performance liquid chromatography coupled with amino acid analysis showed that aloe glycoprotein cleaves the Pro7-Phe8 and Phe8-Arg9 bonds of the bradykinin molecule. The proteolytic action suggests that aloe glycoprotein has carboxypeptidase N- and P-like activity.