Publication | Open Access
Transport of organic compounds in the mammal. Partition of dieldrin and telodrin between the cellular components and soluble proteins of blood
74
Citations
12
References
1964
Year
Pharmaceutical ScienceBioorganic ChemistryRat-epididymal PreparationPolysaccharideEnzymatic ModificationCellular PhysiologyPharmaceutical ChemistryHeme TraffickingMembrane TransportBioanalysisInhibitory ActivityOrganic CompoundsAnimal PhysiologyLimpet PreparationBiochemistryHeme TransportMembrane BiologyPharmacologySoluble Proteins7-1 MmCellular ComponentsNatural SciencesPhysiologyCellular BiochemistryMetabolismMedicine
2. Mannono-(1-+5)-lactone caused 50 % inhibi- tion of the hydrolysis of 6 mM-p-nitrophenyl a-mannoside at 0-080 mm by a rat-epididymal preparation and at 0x098 mm by a limpet prepara- tion.The concentration for 50 % inhibition of the hydrolysis of 2*5 mM-phenyl ,B-mannoside by the limpet preparation was 0-013 mi.3. Concentrations of mannono-(1--4)-lactone causing 50 % inhibition under the same conditions were 40 mm for rat-epididymal a-mannosidase, 26 mm for limpet oc-mannosidase and 7-1 mm for limpet ,-mannosidase.4. Both mannonolactones acted competitively on rat-epididymal ac-mannosidase, with values for Ki of 32 and 0-071 mm for the (1-*4)-and the (1-÷5)-lactone respectively.5. Glucono-(1--*5)-lactone caused 50 % inhibi- tion of the hydrolysis of 6 mM-p-nitrophenyl oc-mannoside at 8-2 mm by the rat-epididymal preparation, and of 5 mM-phenyl a-glucoside at 0-85 mm by the same preparation.With the limpet preparation the concentrations for 50 % inhibition of the hydrolysis of 5 mM-o-nitrophenyl ,B-glucoside and 5 mM-phenyl a-glucoside were 0-092 and 2-2 mm respectively.6. Concentrations of glucono -(1-4) -lactone causing 50 % inhibition under the same conditions were 23 mm for rat-epididymal oc-mannosidase, 1-3 mm for epididymal oc-glucosidase, 0-24 mm for limpet P-glucosidase and 3-2 mm for limpet ac-glucosidase.7. Neither mannono-( 1-4)nor mannono-(l1-5)- lactone caused any inhibition of the limpet /1- glucosidase, and they were alike in their very feeble inhibitory power towards rat-epididymal a-glucosidase.
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