Possible Interaction: Trypsin and Urea

“As well with native protein as with its fragment, complexes formed with trypsin can be dissociated by urea or sodium dodecyl sulfate.”

“The soybean inhibitor trypsin complex dissociates at pH 7.6 in the presence of urea.”

“It is concluded that urea disrupts interaction between the two domains, increasing the accessibility of the interdomain tether that can be digested by trypsin.”

“Inactivation of modified trypsin by urea is less noticeable.”

“The neurite outgrowth activity is relatively stable at pH 3-7 and under denaturing conditions of 8 M urea and beta-mercaptoethanol, but is inactivated by treatment of trypsin.”

“The inhibitor activity was decreased by 27% when heat-treated, 33% when treated with 6 M urea and was almost completely lost when treated with trypsin.”

“In contrast, the caseinolytic activity of trypsin showed a marked increase in presence of urea.”

“Following conjugation, the stability of trypsin in the presence of protein denaturants such as urea and sodium dodecyl sulfate was markedly increased, and the enzyme became resistant to inhibition by naturally-occurring protease inhibitors [2,3] .”

“From various changes in enzymatic activity caused by urea and trypsin perturbation, it is proposed that the conversion of protein kinase from the cAMP dependent to the independent form is due primarily to preferential modification of the regulatory subunit of the holoenzyme.”

“Here we report that in the presence of urea, trypsin can cleave the amino-terminal 67 residues of the plug of the TonB-dependent transporter FhuA, as assessed by gel shift and mass spectrometry assays.”