A prolyl endopeptidase of Sarcophaga peregrina (flesh fly): Its purification and suggestion for its participation in the differentiation of the imaginal discs

Sumio Ohtsuki, Ko Ichi Homma, Shoichiro Kurata, Hiroto Komano, Shunji Natori

Research output: Contribution to journalArticlepeer-review

48 Citations (Scopus)

Abstract

A prolyl endopeptidase that hydrolyses Suc-Gly-Pro-MCA (Sue, succinyl; MCA, methyl-coumaryl-7-amide) was purified to near homogeneity from NIH-Sape-4 cells derived from the flesh fly (Sarcophaga peregrina). The molecular mass of the purified enzyme was 84 kDa, and its activity was inhibited almost completely by 1 mM diisopropyl fluorophos-phate (DFP). Immunoblotting and DFP-labeling experiments revealed that the leg imaginal discs of Sarcophaga contained this enzyme as a major serine proteinase. This prolyl endopeptidase is suggested to be involved in the differentiation of imaginal discs, because 2 mM DFP and 0.1 mM N-benzyloxycarbonyl-thioprolyl-thioprolynal-dimethylacetal (ZTTA), a specific inhibitor for prolyl endopeptidase, inhibited differentiation of the imaginal discs from the eversion to the elongation stage.

Original languageEnglish
Pages (from-to)449-453
Number of pages5
JournalJournal of biochemistry
Volume115
Issue number3
DOIs
Publication statusPublished - 1994 Mar
Externally publishedYes

Keywords

  • Differentiation
  • Imaginal disc
  • Prolyl endopeptidase
  • Sarcophaga peregrina

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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