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

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.

journal_name

J Dermatol Sci

authors

Oono T,Yasutomi H,Ohhashi T,Kodama H,Arata J

doi

10.1016/0923-1811(90)90588-5

subject

Has Abstract

pub_date

1990-09-01 00:00:00

pages

319-23

issue

5

eissn

0923-1811

issn

1873-569X

pii

0923-1811(90)90588-5

journal_volume

1

pub_type

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