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Isolation and partial characterization of a kallikrein from mouse submaxillary glands.

G Porcelli, Costantino Cozzari, Di Iorio M, Croxatto Rh, P. U. Angeletti

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Abstract

A simple procedure to obtain relatively large amounts of purified kallikrein from male mouse submaxillary gland is described. Some chemical and biological properties of this kallikrein have been investigated. The enzyme has a m.w. of 32,000 and shows strong BAEE-esterase activity, as well as kininogenase activity. It is partially inhibited by Aprotinin.

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What this paper is about

A simple procedure to obtain relatively large amounts of purified kallikrein from male mouse submaxillary gland is described. Some chemical and biological properties of this kallikrein have been investigated. The enzyme has a m.w. of 32,000 and shows strong BAEE-esterase activity, as well as kininogenase activity. It is partially inhibited by Aprotinin.

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Available abstract

A simple procedure to obtain relatively large amounts of purified kallikrein from male mouse submaxillary gland is described. Some chemical and biological properties of this kallikrein have been investigated. The enzyme has a m.w. of 32,000 and shows strong BAEE-esterase activity, as well as kininogenase activity. It is partially inhibited by Aprotinin.

Key concepts: Submaxillary gland, Kallikrein, Chemistry, Aprotinin, Esterase, Submandibular gland, Isolation (microbiology), Enzyme

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Isolation and partial characterization of a kallikrein from mouse submaxillary glands. — Research Paper | ScholarLens