Abstract: This research was done to study the effect of changes in pH on the binding characteristics of paracetamol to bovine serum albumin at 37oC as a follow up to the work done previously by Okoro, et al (2015) on this title at 260C .The binding characteristics were investigated at a pH range of 6.0-8.0 using UV- Spectroscopy . The result showed that the binding of paracetamol to bovine serum albumin was impaired at almost neutral and near alkaline pH (6.8 -7.2) with the drug-protein binding constants (KL) of 1.698X102, 0.330X102 and 5.007X102 respectively and was enhanced at higher alkaline pH of 8.0, with the drug-protein binding constant K. of 216,432x102 . This can be interpreted as conformation changes (neutral-base transition change that occurred at pH of 6.8 to 7.2. This confirmed that bovine serum albumin has two structures, one at the acidic pH and the other at the basic pH.