Evidence for biosynthesis of lactase-phlorizin hydrolase as a single-chain high-molecular weight precursor

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Standard

Evidence for biosynthesis of lactase-phlorizin hydrolase as a single-chain high-molecular weight precursor. / Skovbjerg, H; Danielsen, E M; Noren, Ove; Sjöström, H.

I: BBA General Subjects, Bind 798, Nr. 2, 1984, s. 247-51.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Skovbjerg, H, Danielsen, EM, Noren, O & Sjöström, H 1984, 'Evidence for biosynthesis of lactase-phlorizin hydrolase as a single-chain high-molecular weight precursor', BBA General Subjects, bind 798, nr. 2, s. 247-51.

APA

Skovbjerg, H., Danielsen, E. M., Noren, O., & Sjöström, H. (1984). Evidence for biosynthesis of lactase-phlorizin hydrolase as a single-chain high-molecular weight precursor. BBA General Subjects, 798(2), 247-51.

Vancouver

Skovbjerg H, Danielsen EM, Noren O, Sjöström H. Evidence for biosynthesis of lactase-phlorizin hydrolase as a single-chain high-molecular weight precursor. BBA General Subjects. 1984;798(2):247-51.

Author

Skovbjerg, H ; Danielsen, E M ; Noren, Ove ; Sjöström, H. / Evidence for biosynthesis of lactase-phlorizin hydrolase as a single-chain high-molecular weight precursor. I: BBA General Subjects. 1984 ; Bind 798, Nr. 2. s. 247-51.

Bibtex

@article{70a050a0e7be11ddbf70000ea68e967b,
title = "Evidence for biosynthesis of lactase-phlorizin hydrolase as a single-chain high-molecular weight precursor",
abstract = "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).",
author = "H Skovbjerg and Danielsen, {E M} and Ove Noren and H Sj{\"o}str{\"o}m",
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",
year = "1984",
language = "English",
volume = "798",
pages = "247--51",
journal = "B B A - General Subjects",
issn = "0304-4165",
publisher = "Elsevier",
number = "2",

}

RIS

TY - JOUR

T1 - Evidence for biosynthesis of lactase-phlorizin hydrolase as a single-chain high-molecular weight precursor

AU - Skovbjerg, H

AU - Danielsen, E M

AU - Noren, Ove

AU - Sjöström, H

N1 - 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

PY - 1984

Y1 - 1984

N2 - 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).

AB - 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).

M3 - Journal article

C2 - 6143571

VL - 798

SP - 247

EP - 251

JO - B B A - General Subjects

JF - B B A - General Subjects

SN - 0304-4165

IS - 2

ER -

ID: 9881391