• Home
  • Search Results
  • Purification and characterization of a novel prolyl aminopeptidase from Maitake (Grifola frondosa).

Purification and characterization of a novel prolyl aminopeptidase from Maitake (Grifola frondosa).

Bioscience, biotechnology, and biochemistry (2004-06-25)
Kazuyuki Hiwatashi, Kazuyuki Hori, Keitaro Takahashi, Akira Kagaya, Shunzo Inoue, Toshihiro Sugiyama, Saori Takahashi
ABSTRACT

We have found a novel prolyl aminopeptidase in Grifola frondosa. The enzyme was purified by DEAE-Sepharose CL-6B, Butyl-Toyopearl, Sephacryl S-100, and Mono-Q column chromatographies. The purified enzyme exists as a dimer and gives high activity toward L-proline-p-nitroanilide. The enzyme was strongly inhibited by p-chloromercuribenzoic acid and iodoacetic acid and markedly inhibited by phenylmethylsulfonyl fluoride and arphamenin A.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
L-Proline p-nitroanilide trifluoroacetate salt, prolyl aminopeptidase substrate

Social Media

LinkedIn icon
Twitter icon
Facebook Icon
Instagram Icon

Merck

Research. Development. Production.

We are a leading supplier to the global Life Science industry with solutions and services for research, biotechnology development and production, and pharmaceutical drug therapy development and production.

© 2021 Merck KGaA, Darmstadt, Germany and/or its affiliates. All Rights Reserved.

Reproduction of any materials from the site is strictly forbidden without permission.