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Fig. 5Merge interplay between time and strain-rate which is reflected by the presence of a bell-shaped force-velocity characteristic for retraction process in the retraction velocity at the steady state assay the retraction failure of strain-rate dependent on current applied load. As flow-speed increases (i.e Figure 6. velocity increases), so does the failure force. Moreover, when reloading subsequent to a stretch-failure, retraction velocity is higher (Fig 5.b) because TFP are more stretched by the external load in order to achieve the predetermined level for maximum loading/unloading in terms of normalized time. However, the strain-rate sensitivity of retraction is altered whereas the force-velocity characteristic remains unaffected during this reprocessing.
New pulse-chase experimental techniques allow monitoring of the turnover of the cytoplasmic tail of the major subunit in intact and permeabilized cells. These turn-over values were then compared with inactivated Na,K-ATPase activity. For the first time, it was found that inactivation increases turnover of the cytoplasmic tail of the major subunit C in a pulse-chase experiment by up to 4.6-fold, while 18:0/18:1PS-negative control shows no turnover. By contrast, this turnover rate is unchanged in the presence of both 18:0/18:1PS and the transport inhibitor. Thus, we show that inactivation and 18:0/18:1PS induce a cellular process that is specific for the cytoplasmic tail of the major subunit C in intact and permeabilized E. coli and that 18:0/18:1PS is not involved in this process, distinguishing it from post-translational proteolytic cleavage of Na,K-ATPase activity. In addition, we identify the major cytoplasmic tail of the subunit C and C′ proteins as the cellular target of 18:0/18:1PS. d2c66b5586