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Abstract for Trypsin Gold, Mass Spectrometry Grade
Trypsin Gold, Mass Spectrometry Grade, has been manufactured to provide
maximum specificity. Lysine residues in the porcine trypsin have been modified by
reductive methylation, yielding a highly active and stable molecule that is extremely
resistant to autolytic digestion. The specificity of the purified trypsin is further
improved by TPCK treatment, which inactivates chymotrypsin. The treated trypsin is
then purified by affinity chromatography and lyophilized to yield Trypsin Gold, Mass
Spectrometry Grade.
Trypsin Gold, Mass Spectrometry Grade, has extremely high specific activity.
Modified trypsin is maximally active in the range of pH 7–9 and is reversibly
inactivated at pH <4. It is resistant to mild denaturing conditions such as 0.1%
SDS, 1M urea or 10% acetonitrile and retains 50% of its activity in 2M guanidine HCl. The activity of trypsin is decreased when acidic residues are present on either
side of a susceptible bond. If proline is at the carboxylic side of lysine or
arginine, the bond is almost completely resistant to cleavage by trypsin.
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