Peptides (10–40 μg) were radioiodinated with iodine-125 (Perkin Elmer, Waltham, MA) using chloramine T (20 μg) and the products purified by gel filtration using a Sephadex G-25 size-exclusion matrix (PD10; GE Healthcare) using a mobile phase of 0.1 % w/v gelatin in PBS. The radiochemical purity of all products was determined qualitatively by SDS polyacrylamide gel electrophoresis analyzed by phosphor imaging (Cyclone Storage Phosphor System, PerkinElmer, Shelton, CT).
Sephadex g 25 size exclusion matrix pd10
Manufactured by GE Healthcare
Sephadex G-25 is a size-exclusion matrix used for desalting and buffer exchange. It is a gel filtration medium composed of cross-linked dextran beads. The matrix is designed to effectively separate molecules based on their size, allowing larger molecules to pass through the porous beads while smaller molecules are retained. This makes it a useful tool for the purification and concentration of proteins, peptides, and other macromolecules.
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Lab products found in correlation
3 protocols using sephadex g 25 size exclusion matrix pd10
1
Radioiodination of Peptides
2
Radiolabeling of Peptides with I-125
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Peptides (20–40 μg) were radiolabeled with iodine-125 (125I; Perkin Elmer, Waltham, MA) as previously described [9 (link)]. Briefly, ~ 2 mCi of 125I in buffered sodium phosphate pH 7.6 was mixed with peptide and 20 μg chloramine T in a volume of 10 µL water for 1 min. The reaction was quenched using 20 μg sodium metabisulphite in 10 µL water. Radiolabeled product was separated from free isotope by gel filtration chromatography using a Sephadex G-25 size-exclusion matrix (PD10; GE Healthcare) equilibrated with 0.1% gelatin/PBS. Fractions were collected manually and radioactivity in each measured by gamma counting after which the peak fractions were pooled. Radiochemical purity was assessed qualitatively by estimating the free radioiodide from phosphor images (Cyclone Storage Phosphor System, PerkinElmer, Shelton, CT) of SDS-PAGE gels.
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Radioiodination and Purification of Peptides
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