Affinity chromatography - download pdf or read online

By Sameh Magdeldin

ISBN-10: 9535103253

ISBN-13: 9789535103257

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Sepharose CL-4B; agarose crosslinked with 2,3dibromopropanol and desulphated by alkaline hydrolysis under reductive conditions), polyacrylamide, and magnetic beads (Grodzki & Berenstein, 2010; Hober et al, 2007; Katoh et al, 2007; Tyutyulkova & Paul, 1995). All three proteins bind extensively with the IgG subclass. In general, protein A is more suitable for cat, dog, rabbit and pig IgG whereas protein G is generally more preferable when purifying mouse or human IgG. A combination of protein A and G is also applicable for purifying a wide range of mammalian IgG samples.

For acetylcholine esterase, β-galactosidase, lactate dehydrogenase, β-glucuronidase or D-hydantoinase immobilization. , 2010; Terpe, 2003). 2 Immobilization using avidin-biotin interaction Another strategy for affinity immobilization exploits extraordinarily strong affinity interaction (probably one of the strongest noncovalent interactions between two biomolecules) between vitamin H - biotin (figure 6) and egg white glycoprotein avidin or its bacterial alternative streptavidin originating from Streptomyces avidinii.

A few examples of this type of techniques are mentioned in the following paragraphs. In some cases a very tight relations between these methods and earlier described principles based on fusion protein preparation are evident. e. lectins can be used. This type of posttranslational modification is very common in nature and was observed in many eukaryotes, archaebacteria or even in some prokaryotes. The specificity of above mentioned interactions was many times exploited in affinity based purification procedures.

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Affinity chromatography by Sameh Magdeldin

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