Biofunctional membranes normally involve the random immobilization of biomolecules to porous, polymeric membranes, often through the numerous lysine residues on the protein. In this process, bioactivity is significantly decreased largely due to different orientations of the biomolecule with respect
Random and site-specific immobilization of catalytic antibodies
β Scribed by Thomas M. Spitznagel; Jeffrey W. Jacobs; Douglas S. Clark
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- English
- Weight
- 810 KB
- Volume
- 15
- Category
- Article
- ISSN
- 0141-0229
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
Proteins carrying genetically attached polyhistidine tails have been purified using affinity precipitation with metal chelates. DNA fragments encoding four or five histidine residues have been genetically fused to the oligomeric enzymes lactate dehydrogenase (Bacillus stearother- mophilus), 0-glucor
A comparison is made of the specific combining sites of a number of lectins and of antibodies with emphasis on those reacting with blood group A, B, and H determinants. The ranges of site sizes and specificities of both groups are similar both from immunochemical studies and from the limited x-ray d