Titlebook: Basic Protein and Peptide Protocols; John M. Walker Book 1994 Humana Press 1994

Thyroxine

SDS Polyacrylamide Gel Electrophoresis of Proteins,d or rod of length roughly proportionate to the protein’s mol wt. Thus, proteins of either acidic or basic p. form negatively charged complexes that can be separated on the bases of differences in charges and sizes by electrophoresis through a sieve-like matrix of polyacrylamide gel.

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Detection of Proteins in Polyacrylamide Gels Using an Ultrasensitive Silver Staining Technique,taining of proteins following gel electrophoresis was a major advance providing a detection sensitivity between 20–200 times higher than methods using CBB R-250, being able to detect about 0.1 ng protein/band.

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Identification of Glycoproteins on Nitrocellulose Membranes and Gels,uction of disulfide bonds yields a major fragment .. 2–3 × 10.), which we term a subunit. Proteolytic digestion of subunits gives rise to large glycopeptides (.. 300–500,000), which correspond to the very highly-substituted regions of the protein core.

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The Release of Oligosaccharides from Glycoproteins,ype of oligosaccharide present. .-linked chains are more difficult to release as sequential glycosidase digestions (e.g., neuraminidase and .-glycosidase) will remove some but not all types of .-linked chain. For the release of all .-linked chains for further analysis a chemical method is required,