Preparation of Conjugates of Proteins with Amyloses by Elongation of Covalently Attached Primers Using Glycogen Phosphorylase a1
✍ Scribed by Y.H. Chu; G.M. Whitesides
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- English
- Weight
- 588 KB
- Volume
- 21
- Category
- Article
- ISSN
- 0045-2068
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✦ Synopsis
This paper describes convenient preparations of protein-amylose conjugates. These preparations are based on the elongation of maltooligosaccharides by reaction with glucose-1phosphate, catalyzed by glycogen phosphorylase (a). Coupling of maltooligosaccharides to proteins by reductive amination generated covalently attached primers for the glycogen phosphorylase (a)-catalyzed polymerization of glucose-1-phosphate. SDS-polyacrylamide gel electrophoresis was useful for characterizing these conjugates. ({ }^{31}) P NMR spectroscopy could be used conveniently to assay simultaneously the formation and the enzymatic activity of the amylose-conjugated proteins. This assay could be used directly in reactions catalyzed by glycogen phosphorylase (a); it should also be applicable to protein mixtures of greater complexity than the ones used here. Methods of synthesizing enzymatically active neoglycoproteins having a range of molecular weights are described. (\mathcal{E} 1993) Academic Press, Inc