Abstract:
:A wide occurrence of peptide:N-glycanase (PNGase) in mouse organs was demonstrated. PNGase activities were determined using 14C-labeled fetuin glycopeptide I as a substrate by a newly improved enzyme assay based on the paper chromatographic and paper electrophoretic analyses. PNGase activities were detected in both soluble and membranous (or particulate) fractions, although the levels of the activities were different from organ to organ. Soluble PNGases were partially purified from brain, liver, kidney, and spleen by TSK butyl-Toyopearl 650 M hydrophobicity chromatography and characterized for enzymatic properties. The soluble enzymes were found to share the following properties: (a) high hydrophobicity; (b) sensitivity to metal cations such as Zn2+, Cu2+, and Fe3+; and (c) requirement of sulfhydryl group(s) for enzyme activity. Notably, soluble PNGases were unable to degrade glycoasparagine substrates and the optimal pH was near 7.0, suggesting that they were not lysosomal enzymes, but perhaps being involved in basic biological processes in certain intracellular nonlysosomal events. All of these enzymatic properties found for mouse organ-derived PNGases were the same as those recently found for L-929 PNGase that was highly purified as a soluble enzyme from mouse fibroblast L-929 cells (Suzuki, T., Seko, A., Kitajima, K., Inoue, Y., and Inoue, S. (1994) J. Biol. Chem. 269, 17611-17618.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Kitajima K,Suzuki T,Kouchi Z,Inoue S,Inoue Ydoi
10.1006/abbi.1995.1309subject
Has Abstractpub_date
1995-06-01 00:00:00pages
393-401issue
2eissn
0003-9861issn
1096-0384pii
S0003-9861(85)71309-4journal_volume
319pub_type
杂志文章abstract::The present paper focussed on the mechanistic aspect of the reaction of singlet oxygen (1O2), in its lowest excited state (1 Delta g), toward DNA constituents. It is well known that 1O2 is able to react with the guanine moiety of DNA to produce almost specifically 8-oxo-7,8-dihydro-2'-deoxyguanosine (8-oxodGuo). Howev...
journal_title:Archives of biochemistry and biophysics
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journal_title:Archives of biochemistry and biophysics
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
doi:10.1016/j.abb.2008.02.011
更新日期:2008-04-15 00:00:00
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pub_type: 杂志文章
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pub_type: 杂志文章
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更新日期:1990-03-01 00:00:00
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pub_type: 杂志文章
doi:10.1016/j.abb.2020.108314
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pub_type: 杂志文章
doi:10.1016/j.abb.2007.12.004
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
doi:10.1006/abbi.1993.1375
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