Presence in human cells and tissues of two prolidases and their alteration in prolidase deficiency

Two forms of prolidase can be separated for all the human cells and tissues examined by DEAE-cellulose column chromatography or batch methods. Serum had a very low prolidase activity eluting as a single peak prior to tissue peak I prolidase. Analysis of the two peaks can readily be carried out using...

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Bibliographic Details
Published inJournal of inherited metabolic disease Vol. 8; no. 4; p. 193
Main Authors Butterworth, J, Priestman, D A
Format Journal Article
LanguageEnglish
Published United States 01.12.1985
Subjects
Cells, Cultured
Chromatography, DEAE-Cellulose
Dipeptidases - analysis
Dipeptidases - deficiency
Dipeptidases - metabolism
Dipeptides - metabolism
Fibroblasts
Hot Temperature
Humans
Hydroxymercuribenzoates - pharmacology
Infant
Kinetics
Male
Manganese - pharmacology
Tissue Distribution
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Summary:Two forms of prolidase can be separated for all the human cells and tissues examined by DEAE-cellulose column chromatography or batch methods. Serum had a very low prolidase activity eluting as a single peak prior to tissue peak I prolidase. Analysis of the two peaks can readily be carried out using white blood cells, cultured skin fibroblasts and amniotic fluid cells. Dialysis inactivated peak II prolidase although the loss can be prevented by the presence of dithiothreitol. The two peaks differed in their response to Mn(2+), substrate specificity, heat stability and inhibition by p-hydroxymercuribenzoate. In two unrelated cases of prolidase deficiency, fibroblast peak I was markedly reduced, although still detectable, whereas peak II was active against all the substrates, except for a 90% reduction against glycyl-L-proline. The properties of peak II were altered in the disease. The results imply that the two forms of prolidase are structurally related.
ISSN:0141-8955
DOI:10.1007/BF01805434