Characterization of fibroblast-derived prolidase. The presence of two forms of prolidase.
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.
Oono
T
T
Department of Dermatology, Okayama University Medical School, Japan.
Yasutomi
H
H
Ohhashi
T
T
Kodama
H
H
Arata
J
J
D000293:Adolescent; D002478:Cells, Cultured; D002851:Chromatography, High Pressure Liquid; D004150:Dipeptidases / Q000032:analysis* / Q000378:metabolism / Q000502:physiology; D005260:Female; D005347:Fibroblasts / Q000737:chemistry* / Q000201:enzymology / Q000502:physiology; D006801:Humans; D008970:Molecular Weight; D012867:Skin / Q000166:cytology* / Q000201:enzymology; D012879:Skin Physiological Phenomena; D013379:Substrate Specificity / Q000502:physiology
D004150:Dipeptidases; C022449:proline dipeptidase