Solid-phase enzyme modification via affinity chromatography
نویسندگان
چکیده
منابع مشابه
Selective enzyme purification by affinity chromatography.
The purification of proteins by conventional procedures is frequently laborious and incomplete, and the yields are often low. Enzyme isolation based on a highly specific biological property-strong reversible association with specific substrates or inhibitors-has received only limited attention.‘-’ In affinity chromatography, the enzyme to be purified is passed through a column containing a cros...
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M1 RNA, the catalytic subunit of Escherichia coli RNase P, has been covalently linked at its 3' terminus to agarose beads. Unlike M1 RNA, which is active in solution in the absence of the protein component (C5) of RNase P, the RNA linked to the beads is active only in the presence of C5 protein. Affinity chromatography of crude extracts of E. coli on a column prepared from the beads to which th...
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A solid phase immunoadsorbent specific for RNA-dependent DNA polymerase from murine and feline RNA tumor viruses has been prepared. The enzymes from murine and feline virus but not from avian virus bind to columns of this material. Bound enzymes can be eluted in active form. This method has permitted selective purification of viral enzyme from crude extracts of virus-transformed cells, since th...
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Preparation of an agarose derivative (MPE-agarose) containing a maleimido group which is attached to agarose via a cleavable phenyl ester linkage is described. MPE-agarose was shown to react with the thiol groups in glutathione, bovine serum albumin, bovine hemoglobin, and yeast and rabbit muscle glyceraldehyde 3-phosphate dehydrogenase. Treatment of the resulting agarose-linked compounds for 1...
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ژورنال
عنوان ژورنال: Journal of Chromatography B
سال: 2003
ISSN: 1570-0232
DOI: 10.1016/s1570-0232(03)00487-2