Studies on kinetic properties of acid phosphatase from nuclei-free rat liver homogenate using different substrates.

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dc.contributor.authorPandya, Jignesh Den_US
dc.contributor.authorPatel, Bhavesh Den_US
dc.contributor.authorKatewa, Subhash Den_US
dc.contributor.authorKatyare, Surendra Sen_US
dc.date.accessioned2009-05-28T12:35:37Z
dc.date.available2009-05-28T12:35:37Z
dc.date.issued2003-03-23en_US
dc.description.abstractKinetic properties of rat liver acid phosphatase were evaluated using the conventional synthetic substrates sodium beta glycerophosphate (betaGP) and p-nitrophenyl phosphate (PNPP) and physiologically occurring phosphate esters of carbohydrates, vitamins and nucleotides. The extent of hydrolysis varied depending on the substrates; phosphate esters of vitamins and carbohydrates were in general poor substrates. Kinetic analysis revealed the presence of two components of the enzyme for all the substrates. Component I had low Km and low Vmas. Opposite was true for component II. The Km values were generally high for betaGP, PNPP and adenosine diphosphate (ADP). Amongst the nucleotides substrates AMP showed high affinity i.e. low Km. The increase in enzyme activity in general at high substrate concentration seems to be due to substrate binding and positive cooperativity. AMP which showed highest affinity was inhibitory at high concentration beyond 1 mM. The results suggest that in situ the nucleotides may be the preferred substrates for acid phosphatase.en_US
dc.description.affiliationDepartment of Biochemistry, Faculty of Science, M. S. University of Baroda, Vadodara 390 002, India. pandyajignes@hotmail.comen_US
dc.identifier.citationPandya JD, Patel BD, Katewa SD, Katyare SS. Studies on kinetic properties of acid phosphatase from nuclei-free rat liver homogenate using different substrates. Indian Journal of Experimental Biology. 2003 Mar; 41(3): 205-10en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/58292
dc.language.isoengen_US
dc.source.urihttps://www.niscair.res.in/ScienceCommunication/ResearchJournals/rejour/ijeb/ijeb0.aspen_US
dc.subject.meshAcid Phosphatase --metabolismen_US
dc.subject.meshAnimalsen_US
dc.subject.meshKineticsen_US
dc.subject.meshLiver --enzymologyen_US
dc.subject.meshMaleen_US
dc.subject.meshRatsen_US
dc.subject.meshSubstrate Specificityen_US
dc.titleStudies on kinetic properties of acid phosphatase from nuclei-free rat liver homogenate using different substrates.en_US
dc.typeJournal Articleen_US
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