I've recently conducted an experiment on acid and enzyme hydrolysis of ATP. The extent of hydrolysis was measured by calculating the number of mole of phosphates in the solution using Allen phosphate determination. Here, a set of standard solution with number of mole of phosphates ranging from 0-1 μ mole was set up and a standard curve of absorbance against phosphates concentration was plotted.
While i understand how enzymatic hydrolysis occurs, i'm unsure about acid hydrolysis of ATP. And i couldn't find much information on the internet either.I was wondering can anyone explain the basis of acid hydrolysis of ATP to me and which bonds in the ATP was broken during the process?
I was also asked to comment briefly on the acid stability of the various phosphates bonds in the ATP. Some hints for this would be very helpful!
in addition, if i was given a 2.5 mL solution containing 3 μ mole of phosphates, which is clearly out of range of the standard curve i've plotted, how could i accurately determine the phosphate concentration in this sample?
For this question, other than diluting the sample, is there other ways to do this?
Thanks in advance!