๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Purification of epidermal G2-chalone by immunoaffinity chromatography

โœ Scribed by S. A. Ketlinskii; A. S. Simbirtsev

Publisher
Springer US
Year
1983
Tongue
English
Weight
568 KB
Volume
96
Category
Article
ISSN
0007-4888

No coin nor oath required. For personal study only.

๐Ÿ“œ SIMILAR VOLUMES

Partial purification of epidermal G2chal
Partial purification of epidermal G2chalone
โœ G. Isaksson-Forsรฉn; D. R. Burton; R. Korsgaard; K. Elgjo; O. H. Iversen ๐Ÿ“‚ Article ๐Ÿ“… 1978 ๐Ÿ› Springer-Verlag ๐ŸŒ English โš– 379 KB
Purification of swine kidney alkaline ph
Purification of swine kidney alkaline phosphatase by immunoaffinity chromatography
โœ Shinichiro Oida; Masae Sone; Satoshi Sasaki ๐Ÿ“‚ Article ๐Ÿ“… 1984 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 280 KB

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

Purification of recombinant proteins by
Purification of recombinant proteins by immunoaffinity chromatography with preselected antibodies
โœ Jytte Pedersen; Claus Emborg; Jane Sรธrensen; Kirsten Biedermann ๐Ÿ“‚ Article ๐Ÿ“… 1993 ๐Ÿ› Springer-Verlag ๐ŸŒ English โš– 609 KB

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