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pubmed:abstractText |
The procedures summarized above provide nearly homogeneous preparations of IF-2mt, EF-Tu. Tsmt, and EF-Gmt. The scheme developed for IF-2mr leads to a 24,000-fold purification of this factor with a 26% recovery of activity. Analysis by SDS-polyacrylamide gel electrophoresis and gel filtration chromatography indicates that this factor functions as a monomer with a molecular weight of about 85,000. The scheme developed EF-Tu.Tsmt provides a 10,000-fold purification with an overall yield of about 10%. The EF-Tumt component in this complex has a molecular weight of about 46,000, whereas EF-Tsmt has a molecular weight of about 32,000 on SDS-polyacrylamide gel electrophoresis. The EF-Tu. Tsmt complex is tightly associated and appears to have a native molecular weight of about 70,000. The five-step purification procedure outlined above for EF-Gmt results in a 14,000-fold purification of EF-Gmt with a 2-5% recovery of activity. Analysis by SDS-polyacrylamide gel electrophoresis and gel filtration chromatography indicates that EF-Gmt functions as a monomeric protein with an apparent molecular weight of about 80,000.
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