The literatire supplied by GE Healthcare, the manufacturer of Sephacryl resins,
ID: 211426 • Letter: T
Question
The literatire supplied by GE Healthcare, the manufacturer of Sephacryl resins, provides information concerning the fractionation range of the various S-type resins. This information is presented in tems of the molecular weights of globular proteins and dextrans that can be fractionated by these columns. For instance, the fractionation range of Sephacryl S-300HR is 10,000-1,500,000 for globular proteins and 2,000-400,000 for dextrans. Why does the fractionation range for globular proteins and dextrans differ?
Explanation / Answer
Sephacryl S300 -high resolution fractionation range for globular proteins ( which are basically polymers )is MW range 10- 1500 KDa (purifying immunoglobulins , signal transduction proteins,serum proteins, structural proteins like actin and Tubulin ,transporters ,mid sized proteins )
While sephacryl s300 - high resolution fractionation range for dextran proteins ( which are polymers of glucose whose size range to maximum from 3-2000 KDa) is MW range of 1- 400 KDa.
There is the difference in this fractionation range because of the sizes .,solubility in water .,their eluting from the column of chromatography ., and the sieve pore formed by the bis acrlyamide ( sephacryl s300HR) and the conditions in which they are used e.g.., dextrans elution is necessary in the department of microsurgery and pharmacology than in the protein folding and unfolding of the globular proteins..
hydrophobic interior and hydrophilic exterior of globular proteins which explains the solubility of the proteins
and the complete hydrophilic nature Of the dextrans completely soluble and small size gives the difference in The fractionation range ..
Related Questions
Navigate
Integrity-first tutoring: explanations and feedback only — we do not complete graded work. Learn more.