3/14/2024 0 Comments Xee usa![]() All translation products were identified by -methionine labeling, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and fluorography. Cell-free production of the following proteins were used to assess posttranslational modifications: Escherichia coli beta-lactamase for signal sequence cleavage, Saccharomyces cerevisiae alpha-mating factor for translocation and N-linked glycosylation, the soluble protein luciferase for functional activity, and the membrane-bound human insulin receptor for translation efficiency. The in vitro translocation and processing of XEE was examined with a cell-free translation system containing reticulocyte lysate, and appropriate messenger ribonucleic acid (RNA) or complementary deoxyribonucleic acid plasmids with RNA polymerase. The eggs were then dejellied in 2% L-cysteine-HCl and the cytoplasm extracted by centrifugation at 10,000 rpm for 15 min. The XEE was prepared from eggs laid by adult female frogs that received serial injections of gonadotropins. We present the characterization of Xenopus egg extract (XEE) translocation and processing of proteins synthesized in rabbit reticulocyte lysate. Cell-free translation/translocation systems are broadly applied to examine gene expression and characterize the structure-function relationship of gene products. ![]()
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