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

H Skovbjerg; E M Danielsen; Ove Noren; H Sjöström

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

H Skovbjerg, E M Danielsen, Ove Noren, H Sjöström

37 Citations (Scopus)

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).

Original language	English
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

Cite this

@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",

}

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

SN - 0304-4165

VL - 798

SP - 247

EP - 251

JO - B B A - General Subjects

JF - B B A - General Subjects

IS - 2

ER -

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

Abstract

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