A human serum aminopeptidase capable of splitting juxtaterminal bonds involving proline. Basic characteristics, normal values and clinical variations
Human serum was shown to contain an aminopeptidase which is capable of cleaving glycyl-proline from glycyl-proline naphthylamide and from glycyl-prolylalanine. Some additional dipeptide naphthylamides were cleaved slowly and monoamino acid naphthylamides minimally. The peptidase was separated from e...
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Published in: | Clinica chimica acta 1970-04, Vol.28 (1), p.25-36 |
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Main Authors: | , , |
Format: | Article |
Language: | eng |
Subjects: | |
Online Access: | Get full text |
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Summary: | Human serum was shown to contain an aminopeptidase which is capable of cleaving glycyl-proline from glycyl-proline naphthylamide and from glycyl-prolylalanine. Some additional dipeptide naphthylamides were cleaved slowly and monoamino acid naphthylamides minimally. The peptidase was separated from enzymes hydrolysing monoamino acid naphthylamides,
e.g. leucine naphthylamide, by using DEAE cellulose chromatography and gel filtration on Sephadex G-200. The enzyme was optimally active at pH 7.8, did not require metal ions of sulfhydryl groups for activity and was inhibited by high ionic concentrations. Enzyme activity values in sera obtained from unselected hospitalized patients showed a considerably greater variation than did the activity in sera from healthy persons. Low values were measured in patients with rheumatoid arthritis. No correlation between the activity levels of serum glycyl-proline naphthylamide and leucine naphthylamide hydrolysing enzymes was found in the unselected patient material tested. |
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ISSN: | 0009-8981 1873-3492 |