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Gene Review:

APOH - apolipoprotein H (beta-2-glycoprotein I)

Bos taurus

Li, Q.G. et al., Cai, G. et al., Cai, G. et al., Yamada, M. et al., Ye, X.Y. et al., et al.

Ambrozic, Avicin, Ichikawa, Kveder, Matsuura, Hojnik, Atsumi, Rozman, Koike,

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High impact information on APOH

In addition, several low-abundance proteins including fibrinogen beta-chain, chitinase 3-like 1, alpha-antitrypsin, complement C3 alpha-chain, gelsolin and apolipoprotein H were observed only in colostrum [1].
Isolation from fetal bovine serum of an apolipoprotein-H-like protein which inhibits thymidine incorporation in fetal calf erythroid cells [2].
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 [2].
Anti-beta(2)GPI in children with AD were exclusively of the IgG1 subclass and bound to bovine beta(2)GPI as well, but not to either beta(2)GPI combined with the phospholipid cardiolipin [3].
The nucleotide sequence of the ApoH cDNA encoding the bovine apolipoprotein H (ApoH) has been determined [4].

Biological context of APOH

A new whey protein designated apolipoprotein H-like whey protein, with a molecular weight of 62 kDa and an N-terminal amino acid sequence similar to that of apolipoprotein H, was isolated from bovine milk [5].

Anatomical context of APOH

The final purified endothelial cell viability maintaining factor has a molecular weight of 65,000 (reduced) and has been identified as bovine apolipoprotein H by amino-terminal amino acid sequence analysis and Western blot analysis [6].

Associations of APOH with chemical compounds

Purification of apolipoprotein H by polyethylene glycol precipitation [7].

Analytical, diagnostic and therapeutic context of APOH

A new method of polyethylene glycol precipitation followed by heparin affinity chromatography was established to purify apolioprotein H (Apo H, beta 2-glycoprotein I) [7].

References

Identification of low-abundance proteins of bovine colostral and mature milk using two-dimensional electrophoresis followed by microsequencing and mass spectrometry. Yamada, M., Murakami, K., Wallingford, J.C., Yuki, Y. Electrophoresis (2002) [Pubmed]
Isolation from fetal bovine serum of an apolipoprotein-H-like protein which inhibits thymidine incorporation in fetal calf erythroid cells. Li, Q.G., Blacher, R., Esch, F., Congote, L.F. Biochem. J. (1990) [Pubmed]
Anti-beta(2)-glycoprotein I antibodies in children with atopic dermatitis. Ambrozic, A., Avicin, T., Ichikawa, K., Kveder, T., Matsuura, E., Hojnik, M., Atsumi, T., Rozman, B., Koike, T. Int. Immunol. (2002) [Pubmed]
Sequence of a cDNA encoding bovine apolipoprotein H. Gao, B., Virmani, M., Romm, E., Lazar-Wesley, E., Sakaguchi, K., Appella, E., Kunos, G., Takács, L. Gene (1993) [Pubmed]
Purification of a novel apolipoprotein H-like milk protein with ribonucleolytic and cell-free translation inhibitory activities. Ye, X.Y., Ng, T.B. Life Sci. (2000) [Pubmed]
Purification and characterization of an endothelial cell-viability maintaining factor from fetal bovine serum. Cai, G., Satoh, T., Hoshi, H. Biochim. Biophys. Acta (1995) [Pubmed]
Purification of apolipoprotein H by polyethylene glycol precipitation. Cai, G., Guo, Y., Shi, J. Protein Expr. Purif. (1996) [Pubmed]

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