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Enzyme Research
Reports from T. Takenawa and co-researchers add new data to research in enzyme research
June 15th, 2009
According to recent research from Tsukuba, Japan, "An LC-MS study revealed some heterogeneity in terms of molecular mass of a cysteine-free mutant of dihydrofolate reductase (DHFR) after long storage of the highly purified protein as an ammonium sulfate precipitate, but not in the case of a cysteine- and methioneine-free mutant of DHFR. One-third of the cysteine-free DHFR sample stored for a long time, around 18 months, comprised molecular species with molecular masses increased by 16, 32 and 48 Da." "A peptide mapping study revealed that at least one of the methionine residues at positions 1, 16 and 20 was oxidatively modified to a methione-sulfoxide residue, while...
Source: Proteomics Weekly (2009-06-15)
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