Evidence for biosynthesis of lactase-phlorizin hydrolase as a single-chain high-molecular weight precursor
Research output: Contribution to journal › Journal article › Research › peer-review
Precursor forms of lactase-phlorizin hydrolase, sucrase-isomaltase and aminopeptidase N were studied by pulse-labelling of organ-cultured human intestinal biopsies. After labelling the biopsies were fractionated by the Ca2+-precipitation method and the enzymes isolated by immunoprecipitation. The results indicate that the lactase-phlorizin hydrolase is synthesized as a Mr 245 000 polypeptide, which is intracellularly cleaved into its mature Mr 160 000 form. Sucrase-isomaltase is shown to be synthesized as a single chain precursor (Mr 245 000 and 265 000) while the precursor of aminopeptidase N is shown to be of apparently the same size as the mature enzyme (Mr 140 000 and 160 000).
Original language | English |
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Journal | BBA General Subjects |
Volume | 798 |
Issue number | 2 |
Pages (from-to) | 247-51 |
Number of pages | 4 |
ISSN | 0304-4165 |
Publication status | Published - 1984 |
Bibliographical note
Keywords: Aminopeptidases; Antigens, CD13; Electrophoresis, Polyacrylamide Gel; Enzyme Precursors; Glucosidases; Glycosylceramidase; Humans; Intestine, Small; Molecular Weight; Multienzyme Complexes; Organ Culture Techniques; Sucrase-Isomaltase Complex; beta-Galactosidase
ID: 9881391