Rapid purification of calcium-activated protease by calcium-dependent hydrophobic-interaction chromatography
نویسندگان
چکیده
منابع مشابه
Proteolytic activation of calcium-activated, phospholipid-dependent protein kinase by calcium-dependent neutral protease.
A Ca2+-dependent protease I), which hydrolyzes casein at Ca2+ concentrations lower than the 10(-5) M range, is purified roughly 4000-fold from the soluble fraction of rat brain. This protease is able to activate Ca2+-activated, phospholipid-dependent protein kinase (protein kinase C) by limited proteolysis analogously to the previously known Ca2+-dependent analogously to the previously known Ca...
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This paper describes a method for the plasmid DNA purification, which includes an ammonium sulphate precipitation, followed by hydrophobic interaction chromatography (HIC) using Phenyl Sepharose 6 Fast Flow (low sub). The use of HIC took advantage of the more hydrophobic character of single stranded nucleic acid impurities as compared with double-stranded plasmid DNA.
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The activation mechanism through limited autolysis of a calcium-activated neutral protease (CANP) with a high sensitivity to calcium ions (pCANP) was analyzed. The rate of autolysis was dependent on pCANP concentration. The reaction was inhibited by high concentrations of digestible substrates but not by a nondigestible substrate. Incubation of pCANP inactivated by Nethylmaleimide with a small ...
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The chromatographic methods used for the purification of PEGylated proteins are mainly Size Exclusion (SEC) and Ion Exchange Chromatography (IEX). Although the PEGylation affects the protein hydrophobicity, Hydrophobic Interaction Chromatography (HIC) has not been extensively applied for the separation of these proteins. Purification of monoPEGylated Ribonuclease A (RNase A) using HIC is studie...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1985
ISSN: 0014-5793
DOI: 10.1016/0014-5793(85)80717-1