1. Albumin-like glycoprotein from human fetal tissue.
- Author
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Karelin AA, Phylippova MM, Blishchenko EYu, Bovin NV, Nasonov VV, Shiyan SD, Petrova EE, Nesmeyanov VA, Sashchenko LP, and Gnuchev NV
- Subjects
- Animals, Carbohydrate Sequence, Cell Division drug effects, Chromatography, High Pressure Liquid, Glycoproteins metabolism, Glycoproteins pharmacology, Humans, Mice, Mice, Inbred BALB C, Molecular Sequence Data, Molecular Weight, Tumor Cells, Cultured, Tumor Necrosis Factor-alpha antagonists & inhibitors, Tumor Necrosis Factor-alpha toxicity, Vitronectin, Glycoproteins chemistry, Serum Albumin chemistry
- Abstract
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.
- Published
- 1994