| Autor: |
S, Ishii, R, Kase, H, Sakuraba, C, Taya, H, Yonekawa, T, Okumiya, Y, Matsuda, K, Mannen, M, Takeshita, Y, Suzuki |
| Rok vydání: |
1999 |
| Předmět: |
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| Zdroj: |
Glycoconjugate journal. 15(6) |
| ISSN: |
0282-0080 |
| Popis: |
We produced six transgenic mouse lines expressing human alpha-galactosidase (alpha-Gal) in order to evaluate its posttranslational modification. Among them, serum alpha-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 alpha-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. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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