An aspartic proteinase from human erythrocytes is immunochemically indistinguishable from a non-pepsin, electrophoretically slow moving proteinase from gastric mucosa

Nadezhda I. Tarasova, Pal B. Szecsi, Bent Foltmann

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    Abstrakt

    Antiserum raised against an erythrocyte membrane-attached aspartic proteinase precipitates a non-pepsin gastric proteinase. With a monospecific antiserum raised against the non-pepsin gastric proteinase the two enzymes show immunochemical identity. The isoelectric points of both are between 4.5 and 4.6. By SDS-polyacrylamide gel electrophoresis the two proteinases behave the same way. Under non-reducing conditions the main components show molecular weights around 90 000 and after reduction about 58 000. The proteinase may tentatively be classified as cathepsin E.

    OriginalsprogEngelsk
    Sider (fra-til)96-100
    Antal sider5
    TidsskriftBBA - General Subjects
    Vol/bind880
    Udgave nummer1
    DOI
    StatusUdgivet - 15 jan. 1986

    Fingeraftryk Udforsk hvilke forskningsemner 'An aspartic proteinase from human erythrocytes is immunochemically indistinguishable from a non-pepsin, electrophoretically slow moving proteinase from gastric mucosa' indeholder.

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