Nuclease produced by recombinant Escherichia coli was successfully purified by immunoafftnity chromatography using an antibody preselected for the purpose on the basis of an elution assay. The elution assay was also used to optimize elution conditions. One step recovery of nuclease from crude peripl
Purification of mouse myelin basic proteins by immunoaffinity chromatography
β Scribed by Linda S. Reidl; Anthony T. Campagnoni
- Book ID
- 107903076
- Publisher
- Elsevier Science
- Year
- 1983
- Tongue
- English
- Weight
- 615 KB
- Volume
- 8
- Category
- Article
- ISSN
- 0165-0270
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
A homogeneous alkaline phosphatase preparation was obtained from swine kidney cortex by a simple purification step of immunoaffinity chromatography. The enzyme was purified 426 times that of the initial acetone powder with a recovery of 69.6% and a specific activity of 1206 units/mg of protein. The
Myelin basic protein (MBP) occurs in multiple forms. Three of these isoforms from human MBP (HMBP) have been highly purified. HMBP, component 1 (18.5 kDa HMBP-l), was purified by ion-exchange chromatography at pH 10.6 in 2 M urea. During this ion-exchange chromatography, a fraction (Fraction 3), whi