HUMAN ASPARTYLGLUCOSAMINIDASE - A BIOCHEMICAL AND IMMUNOCYTOCHEMICAL CHARACTERIZATION OF THE ENZYME IN NORMAL AND ASPARTYLGLUCOSAMINURIA FIBROBLASTS
ENOMAA, N ; HEISKANEN, T ; HALILA, R ; SORMUNEN, R ; SEPPALA, R ; Vihinen, Mauno LU
and PELTONEN, L
(1992)
In Biochemical Journal
286.
p.613-618
- Abstract
- Aspartylglucosaminidase (AGA, EC 3.5.1.26) is an essential enzyme in the degradation of asparagine-linked glycoproteins. In man, deficient activity of this enzyme leads to aspartylglucosaminuria (AGU), a recessively inherited lysosomal storage disease. Here we used affinity-purified polyclonal antibodies against the native AGA and its denatured subunits to establish the molecular structure and intracellular location of the enzyme in normal and AGU fibroblasts. Inactivation of the enzyme was found to coincide with the dissociation of the heterodimeric enzyme complex into subunits. Although the subunits were not linked by covalent forces, the intrapolypeptide disulphide bridges were found to be essential for the normal function of AGA. AGA... (More)
- Aspartylglucosaminidase (AGA, EC 3.5.1.26) is an essential enzyme in the degradation of asparagine-linked glycoproteins. In man, deficient activity of this enzyme leads to aspartylglucosaminuria (AGU), a recessively inherited lysosomal storage disease. Here we used affinity-purified polyclonal antibodies against the native AGA and its denatured subunits to establish the molecular structure and intracellular location of the enzyme in normal and AGU fibroblasts. Inactivation of the enzyme was found to coincide with the dissociation of the heterodimeric enzyme complex into subunits. Although the subunits were not linked by covalent forces, the intrapolypeptide disulphide bridges were found to be essential for the normal function of AGA. AGA was localized into lysosomes in control fibroblasts by both immunofluorescence microscopy and immuno-electron microscopy, whereas in AGU cells the location of antigen was different, suggesting that, owing to the mutation, a missing disulphide bridge, most of the enzyme molecules get retarded in the cis-Golgi region and most probably face intracellular degradation. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3853455
- author
- ENOMAA, N
; HEISKANEN, T
; HALILA, R
; SORMUNEN, R
; SEPPALA, R
; Vihinen, Mauno
LU
and PELTONEN, L
- publishing date
- 1992
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biochemical Journal
- volume
- 286
- pages
- 613 - 618
- publisher
- Portland Press
- external identifiers
-
- wos:A1992JM26200044
- scopus:0026788005
- ISSN
- 0264-6021
- language
- English
- LU publication?
- no
- id
- 48d15739-f8f9-473e-a696-bf49fd6012eb (old id 3853455)
- date added to LUP
- 2016-04-01 16:16:18
- date last changed
- 2021-04-04 04:35:23
@article{48d15739-f8f9-473e-a696-bf49fd6012eb,
abstract = {{Aspartylglucosaminidase (AGA, EC 3.5.1.26) is an essential enzyme in the degradation of asparagine-linked glycoproteins. In man, deficient activity of this enzyme leads to aspartylglucosaminuria (AGU), a recessively inherited lysosomal storage disease. Here we used affinity-purified polyclonal antibodies against the native AGA and its denatured subunits to establish the molecular structure and intracellular location of the enzyme in normal and AGU fibroblasts. Inactivation of the enzyme was found to coincide with the dissociation of the heterodimeric enzyme complex into subunits. Although the subunits were not linked by covalent forces, the intrapolypeptide disulphide bridges were found to be essential for the normal function of AGA. AGA was localized into lysosomes in control fibroblasts by both immunofluorescence microscopy and immuno-electron microscopy, whereas in AGU cells the location of antigen was different, suggesting that, owing to the mutation, a missing disulphide bridge, most of the enzyme molecules get retarded in the cis-Golgi region and most probably face intracellular degradation.}},
author = {{ENOMAA, N and HEISKANEN, T and HALILA, R and SORMUNEN, R and SEPPALA, R and Vihinen, Mauno and PELTONEN, L}},
issn = {{0264-6021}},
language = {{eng}},
pages = {{613--618}},
publisher = {{Portland Press}},
series = {{Biochemical Journal}},
title = {{HUMAN ASPARTYLGLUCOSAMINIDASE - A BIOCHEMICAL AND IMMUNOCYTOCHEMICAL CHARACTERIZATION OF THE ENZYME IN NORMAL AND ASPARTYLGLUCOSAMINURIA FIBROBLASTS}},
volume = {{286}},
year = {{1992}},
}