Biomedical subjects
Publications and source records attributed to J L Strominger.
A method for the partial purification of the uridine diphospho-N-acetylglucosamine-enolpyruvate reductase from Staphylococcus epidermidis is presented. Some properties of the enzyme, including its dependence on monovalent cation and flavine adenine dinucleotide, are discussed.
The enzyme which catalyzes the transfer of glucosyl residues from adenosine diphospho(ADP)-glucose to glycogen has been partially purified from extracts of Pasteurella pseudotuberculosis. In contrast to other glycogen synthetases of this type, guanosine diphospho-glucose had about 5% of the activity of ADP-glucose as a glucosyl donor. Some other properties of the enzyme are described and compared to other bacterial glycogen synthetases.
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