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Isolation from fetal bovine serum of an apolipoprotein-H-like protein which inhibits thymidine incorporation in fetal calf erythroid cells.
- Source :
-
The Biochemical journal [Biochem J] 1990 Apr 01; Vol. 267 (1), pp. 261-4. - Publication Year :
- 1990
-
Abstract
- A 46 kDa heparin-binding protein which inhibits thymidine incorporation in cultures of fetal calf liver erythroid cells was isolated from fetal bovine serum by affinity chromatography on heparin-Sepharose, ion-exchange chromatography, gel filtration and reversed-phase h.p.l.c. The N-terminal sequence of the first 22 amino acids showed 81% identity with the published sequence of human apolipoprotein H. The isolated protein inhibited thymidine incorporation with an ED50 (concn. producing 50% of maximal effect) of 36 nM. A 100% inhibition of thymidine incorporation and a 40% decrease in cell numbers in cultures of fetal calf erythroid cells were observed at a protein concentration of 840 nM. No effects could be seen in cultures of 3T3 cells used as controls. Human apolipoprotein H had no inhibitory activity in any of the cell cultures tested, suggesting a species-specificity or a different structure or function for the bovine heparin-binding protein.
- Subjects :
- Amino Acid Sequence
Animals
Cattle
Cells, Cultured
Chromatography, High Pressure Liquid
Chromatography, Ion Exchange
Glycoproteins pharmacology
Humans
Molecular Sequence Data
Molecular Weight
Sequence Homology, Nucleic Acid
beta 2-Glycoprotein I
Erythrocytes metabolism
Fetal Blood analysis
Fetal Blood cytology
Glycoproteins blood
Thymidine blood
Subjects
Details
- Language :
- English
- ISSN :
- 0264-6021
- Volume :
- 267
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- The Biochemical journal
- Publication Type :
- Academic Journal
- Accession number :
- 2327984
- Full Text :
- https://doi.org/10.1042/bj2670261