NDLI: α-Galactosidase transgenic mouse: Heterogeneous gene expression and posttranslational glycosylation in tissues

Content Provider	Springer Nature Link
Author	Ishii, Satoshi Kase, Ryoichi Sakuraba, Hitoshi Taya, Choji Yonekawa, Hiromichi Okumiya, Toshika Matsuda, Yoichi Mannen, Kazuaki Takeshita, Masazumi Suzuki, Yoshiyuki
Copyright Year	1998
Abstract	We produced six transgenic mouse lines expressing human α-galactosidase (α-Gal) in order to evaluate its posttranslational modification. Among them, serum α-Gal activity increased 3000-fold in two transgenic mouse lines (TgN2 and TgN51), as compared to that in non-transgenic lines. The heart and liver of the TgN2 mouse expressed a high amount of transcript as well as high α-Gal activity. Its gene products in the heart and kidney were sensitive to endoglycosidase H digestion, but those in the spleen and liver were largely resistant. Glycopeptidase F treatment confirmed an identical molecular mass for the peptide moiety of the enzyme. We concluded that heterogeneous molecular mass of the gene products was caused by different degrees of posttranslational glycosylation in murine tissues.
Starting Page	591
Ending Page	594
Page Count	4
File Format	PDF
ISSN	02820080
Journal	Glycoconjugate Journal
Volume Number	15
Issue Number	6
e-ISSN	15734986
Language	English
Publisher	Kluwer Academic Publishers-Plenum Publishers
Publisher Date	1998-01-01
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Pathology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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α-Galactosidase transgenic mouse: Heterogeneous gene expression and posttranslational glycosylation in tissues