Selective affinity chromatography with calmodulin fragments coupled to sepharose.
نویسندگان
چکیده
منابع مشابه
Calcium-dependent affinity chromatography of S-100 and calmodulin on calmodulin antagonist-coupled Sepharose.
Two different calcium-binding proteins, S-100 and calmodulin, have been isolated from bovine brain by calcium-dependent affinity chromatography on calmodulin antagonist coupled to Sepharose. Calmodulin antagonist N-(6-aminohexyl)-5-chloro-l-napthdenesulfonamide (W-7) has been coupled to epoxy-activated Sepharose 6B or cyanogen bromide-acitivated Sepharose 4B. S-100-like protein bound to W-7 cou...
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Pyran covalently linked to cyanogen bromide-activated Sepharose has been shown to be an effective affinity matrix for several viral DNA polymerases. Differential salt elution of viral compared with cellular polymerases, as well as substrate elution, suggests the affinity nature for the matrix. Unlike some other affinity systems described, pyran-Sepharose is totally resistant to nuclease digesti...
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Novobiocin-Sepharose was prepared by coupling of novobiocin to Epoxy-activated Sepharose 6B and used as an affinity adsorbent. Four novobiocin-binding proteins were isolated from crude extracts of Escherichia coli with molecular weights of 105, 92, 85 and 40 kdal. The two larger proteins were identified as the A subunit (gyrA protein) and the B subunit (gyrB protein) of DNA gyrase topoisomerase...
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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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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1985
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)88876-7