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Rapid chromatogrpahic purification of dipeptidyl peptidase IV in human submaxillary gland by Kohichi Kojima; Tokiko Hama; Takeshi Kato; Toshiharu Nagatsu is a Chemistry article available to read on EtoBox.

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Pure dipeptidyl peptidase Lv (x-psolyl dipeptidyl aminopeptidase), wbicb did not contain aminopeptidase activity at all, was rapidly prepared from the human submaxiUary g&nd by chronatogmpby with concanavalia Asepharose and GIy-Pm-NEi-(CH&+EKSepharose. The entire purification took only 3 days. Arninopeptidase, which was very diEcult to separates from dipeptidyl peptidase N by various chromatographic procedmzs, could be completely removed by chromatography with Gly-Fro-NH-(CH&NEMepharose. 0x1 SDS gel ekctrophoresis the pu&xi enzyme gave a single band with a molecuIar weight of 116,000. The apparent mokcular weight of the enzyme was estimated to be 225,000 by gel 6ltration. Therefore the enzynze umsists of two identical subunits-It did not hydrolyze Ala p-nitmanilide at all, but. the hydrolysis of the p-nitroanilides of Gly-Pro, Lys-?ro and Arg-Pro at pH 8.0 was nearly specik lNTEtOlX\_KX'ION In 1966, Hopsu-Havu and Gienner' discovered a new arylamidase, using a newly synthesized chromogenic substrate, Gly-Pro /?-naphthykunide. They designated the enzyme glycylproline &naphtbyla.midase\_ The enzyme was ptied Erom porcine kidne~J, lamb kidney6, porcine small intestine7 and human subma

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Author

Kohichi Kojima; Tokiko Hama; Takeshi Kato; Toshiharu Nagatsu

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 1873-3778)

Published

1980

Language

EN

Field

Chemistry (Physical Sciences)