| Autor: |
Golovanova, N.K., Samovilova, N.N., Gracheva, E.V., Peklo, M.M., Vlasik, T.N., Sobolev, A.Yu., Jurchenko, Yu.V., Prokazova, N.V. |
| Předmět: |
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| Zdroj: |
Biochemistry (00062979); Mar2004, Vol. 69 Issue 3, p275-280, 6p |
| Abstrakt: |
Polyclonal antibody was raised to a cloned fragment of human GM3 synthase. Affinity purified R27C1 antibody to the tagged recombinant protein inhibited GM3 synthase activity in human liver and HL-60 cells in a dose-dependent manner. However, the R27C1 antibody did not affect liver sialyltransferase activity towards asialofetuin. We are the first to measure GM3 synthase activity in human liver (194 ± 60 pmol NeuAc/h per mg protein), which was about 10-fold lower than in phorbol myristate acetate-stimulated HL-60 cells (1353 ± 573 pmol NeuAc/h per mg protein). On immunoblotting the R27C1 antibody recognized a common protein band in a number of human tissues (liver, brain, atherosclerotic aortic intima, HL-60 cells) with molecular mass of about 60 kD, which is similar to that of the purified GM3 synthase from rat liver. In human liver and aortic intima, the 60-kD band was almost a single band, which makes possible the use of the R27C1 anti- body for immunohistochemical studies in these tissues. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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