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Purification and Characterization of Dipeptidyl Aminopeptidase III from Human Placenta

YOSHIMITU SHIMAMORI, YASUHIRO WATANABE, YUKIO FUJIMOTO

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YOSHIMITU SHIMAMORI
YASUHIRO WATANABE
YUKIO FUJIMOTO
Author's Organization：
Department of Clinical Biochemistry, Hokkaido Institute of Pharmaceutical Sciences
Department of Clinical Biochemistry, Hokkaido Insititute of Pharmaceutical Sciences
Department of Clinical Biochemistry, Hokkaido Institute of Pharmaceutical Sciences

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Keywords:human placenta

JOURNALFREE ACCESS

1986 Volume 34Issue 8Pages 3333-3340

DOIhttps://doi.org/10.1248/cpb.34.3333

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Published: August 25, 1986Received: February 27, 1986Available on J-STAGE: March 31, 2008Accepted: -Advance online publication: -Revised: -

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Abstract

Dipeptidyl aminopeptidase III (DAP III) from a human placental post-microsomal supernatant was purified 760-fold by means of ammonium sulfate fractionation and successive chromatographies on diethylaminoethyl (DEAE)-cellulose, Sephadex G-200, Butyl-Toyopearl 650 and DEAE-Toyopearl columns. The enzyme showed a single band on sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis and its molecular weight was estimated to be 84000. The enzyme was strongly inhibited by metallochelators, and the activity lost was most effectively restored by the addition of Zn²⁺. The enzyme was also extremely inhibited by some sulfhydryl reagents such as p-chloromercuribenzoic acid (PCMB) and 5, 5'-dithiobis(2-nitrobenzoic acid) (DTNB), and the activity of the enzyme inhibited by DTNB was restored by the addition of thiol reagents. Among various β-naphthylamides examined, Arg-Arg-β-naphthylamide (Arg-Arg-βNA) was most rapidly hydrolyzed.

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