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Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia
Abstract
[print version]

A.A.Karelin, M.M.Phylippova, E.Yu.Blishchenko, N.V.Bovin, V.V.Nasonov, S.D.Shiyan, E.E.Petrova, V.Nesmeyanov, etc.
Albumin-like glycoprotein from from human fetal tissue.
Biochem. and Molec. Biol. International, 33 (1), pp. 73 - 80, (1994)

Albumin-like glycoprotein (Gp66) with a molecular mass of 66 kDa has been isolated from human fetal tissue by size-exclusion, ion-exchange chromatography and reverse-phase HPLC. Reactivity of Gp66 with antiserum raised against the major protein components fraction of human fetal serum was observed. The N-terminal 35 amino acid residues of Gp66 were identical to human serum albumin. Meanwhile Gp66 differed from albumin by a/ the presence of 3-5 Trp residues instead of 1 according to fluorescence and UV-spectra, b/ the glycosylation pattern: bi-, tri-, and tetraantennary sialooligosaccharides of a complex type were present. Isoelectric focusing revealed 4 isoforms (pI ranging within 4.8 to 5.1) of Gp66. Gp66 (but not asialo-Gp66) was able to inhibit the cytotoxic effect of TNF against the tumor cell line L929. Inhibition of WEHI-3 and L929 tumor cells proliferation by Gp66 was similar to that of albumin.

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