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KMID : 0578319950050050413
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Molecules and Cells
1995 Volume.5 No. 5 p.413 ~ p.418
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Expression and Purification of Mouse Sulfated Glycoprotein-2
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Ji, young-Mi
Lee, kwang-hee/you, Kwan-Hee
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Abstract
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SGP-2 is a glycosylated protein initially found in the testes of rats. The cDNA of SGP-2 isolated from mouse testis was transcribed in vitro using SP6 RNA polymerase and the transcribed RNA product was translated in vitro using rabbit reticulocyte. The molecular weight of the in vitro translated SGP-2 was 41,000, which is 10,000 less than that calculated based on the nucleotide sequence. We proposed that there is an internal signal for translation in front of methionine residue at 92. Based on these results, it was conjectured that SGP-2 could be regulated translationally. The cDNA of SGP-2 was also expressed in E. coli using T7 RNA polymerase system. SGP-2 cDNA was fused to the gene of glutathione-S-transferase, and the fusion protein was purified from E. coli extracts in a single step using affinity chromatography.
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KEYWORD
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