Effects of proteins and polynucleotides on the activity of various hydrolases
- 1 May 1972
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 127 (5) , 795-800
- https://doi.org/10.1042/bj1270795
Abstract
The effect of various macromolecules on the activity of several hydrolases was studied. Dilution of partially purified acid β-galactosidase from ileal mucosa of suckling rats resulted in a decrease of specific activity. The relationship between specific activity and dilution of the enzyme suggests a dissociation of the enzyme. This could be prevented by addition of several proteins tested. However, addition of DNA to the assay mixture for acid β-galactosidase caused an inhibition. This inhibition could be prevented by addition of proteins. Other polynucleotides and tRNA also exert an inhibitory effect that is prevented by albumin, but nucleotides have no effect. This inhibition occurs maximally at a low pH (3.0–4.0); no inhibition is observed at pH5.5. A similar pH-dependent inhibition by DNA was also found with various other acid hydrolases.Keywords
This publication has 10 references indexed in Scilit:
- Developmental changes of β-galactosidase and β-glucuronidase in the rat liver and kidneyArchives of Biochemistry and Biophysics, 1971
- Characteristics of β-galactosidase in the mucosa of the small intestine of infant rats. Physicochemical propertiesBiochemical Journal, 1969
- The development of arylsulphatase in the small intestine of the ratBiochemical Journal, 1969
- A method for the separate assay of “neutral” and “acid” β-galactosidase in homogenates of rat small-intestinal mucosaAnalytical Biochemistry, 1969
- Rat small-intestinal β-galactosidases. Kinetic studies with three separated fractionsBiochemical Journal, 1968
- BETA-GALACTOSIDASE ACTIVITY OF JEJUNUM AND ILEUM OF SUCKLING RATS COMPARISON OF ACTIVITIES OF BETA-GALACTOSIDASE AT DIFFERENT CONCENTRATION OF SUBSTRATES (O-NITROPHENYL-BETA-D-GALACTOSIDE AND LACTOSE) AT DIFFERENT PH1966
- Method for assay of intestinal disaccharidasesAnalytical Biochemistry, 1964
- The mechanism of carbohydrase action. 8. Structures of the muscle-phosphorylase limit dextrins of glycogen and amylopectinBiochemical Journal, 1960
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951
- A Coenzyme of Spleen β-GlucuronidaseScience, 1950