PROTEIN A FROM STAPHYLOCOCCUS-AUREUS - ITS ISOLATION BY AFFINITY CHROMATOGRAPHY AND ITS USE AS AN IMMUNOSORBENT FOR ISOLATION OF IMMUNOGLOBULINS
PROTEIN A FROM STAPHYLOCOCCUS-AUREUS - ITS ISOLATION BY AFFINITY CHROMATOGRAPHY AND ITS USE AS AN IMMUNOSORBENT FOR ISOLATION OF IMMUNOGLOBULINS
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DOI:
10.1016/0014-5793(72)80680-x
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发表时间:
1972-01-01
期刊:
影响因子:
3.5
通讯作者:
SJOQUIST, J
中科院分区:
文献类型:
--
作者:
HJELM, H;HJELM, K;SJOQUIST, J
Protein A from Staphylococcus aureus is covalently linked to the peptidoglycan part of the cell wall [1, 21. It can be released from the cells by digestion with lysostaphin, and this procedure is the initial step in the isolation of the protein from the bacteria [l]. Further purification of the protein has involved acid and salt precipitation, ion exchange chromatography and gel filtration. The yield of protein A by this technique is approx. 5% of the total amount of the protein in the cell [1].Since protein A reacts with the Fc-part of IgG [3, 41, non-immune IgC or Fc from IgG coupled to Sepharose can be used as an immunosorbent for isolation of the protein. Conversely, protein A bound to Sepharose can be used as an immunosorbent for isolation of IgG from several species as well as for the isolation of the Fc-fraction. This article describes the isolation of protein A from S. aureus and of IgG from human serum by affinity chromatography. In addition, several uses for protein A bound to a solid support as an immunosorbknt will be discussed.