Characterization of fibroblast-derived prolidase. The presence of two forms of prolidase

Takashi Oono, Hiroshi Yasutomi, Toshitaka Oohashi, Hiroyuki Kodama, Jirô Arata

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Crude enzyme solutions of prolidase were extracted from cultured human skin fibroblasts derived from control and prolidase-deficient sisters. Two forms of prolidases (prolidase-I and II) were partially purified by high performance liquid chromatography equipped with an ion exchange column. On gel filtration, the relative molecular weights of prolidase-I and II were estimated to be MW = 105,000 and 151,000, respectively. The substrate specificity of partially purified prolidase-I and II in control fibroblasts was estimated against Gly-Pro, Ala-Pro, Met-Pro. Each form of prolidase differed in its substrate specificity. In prolidase-deficient sisters, the elder with typical clinical manifestations and the younger with only slight clinical manifestations, the activity of prolidase-I was absent. However, the activity of prolidase-II was sufficiently present in both sisters. The substrate specificity of prolidase-II in the patients was similar to that of control. No difference in substrate specificity was found between these two patients.

Original languageEnglish
Pages (from-to)319-323
Number of pages5
JournalJournal of Dermatological Science
Volume1
Issue number5
DOIs
Publication statusPublished - 1990

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proline dipeptidase
Fibroblasts
Substrate Specificity
Siblings
Substrates
Ion Exchange

Keywords

  • Fibroblast-derived prolidase
  • High performance liquid chromatography
  • Prolidase deficiency
  • Prolidase-I
  • Prolidase-II

ASJC Scopus subject areas

  • Dermatology

Cite this

Characterization of fibroblast-derived prolidase. The presence of two forms of prolidase. / Oono, Takashi; Yasutomi, Hiroshi; Oohashi, Toshitaka; Kodama, Hiroyuki; Arata, Jirô.

In: Journal of Dermatological Science, Vol. 1, No. 5, 1990, p. 319-323.

Research output: Contribution to journalArticle

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