نتایج جستجو برای: bovine carbonic anhydrase

تعداد نتایج: 79402  

Journal: :journal of physical & theoretical chemistry 2009
all akbar saboury christopher olumuyiwa aboluwoye naghme sarri-sarraf

the ph dependence study reveals that the cys 206 sulphydryl group of bovine carbonicanhydrase in the native form is not exposed. during the reaction of 2,2'-dithiobispyridine (2-dtp) with the enzyme, there was no absorbance change recorded. in the presence ofsurfactants, the ph dependence profiles of the apparent second order rate constants, kapp, forthe reaction of 2-dtp with bovine carbonic a...

Journal: :journal of physical and theoretical chemistry 0
all akbar saboury - christopher olumuyiwa aboluwoye - naghme sarri-sarraf -

the ph dependence study reveals that the cys 206 sulphydryl group of bovine carbonicanhydrase in the native form is not exposed. during the reaction of 2,2'-dithiobispyridine (2-dtp) with the enzyme, there was no absorbance change recorded. in the presence ofsurfactants, the ph dependence profiles of the apparent second order rate constants, kapp, forthe reaction of 2-dtp with bovine carbo...

All Akbar Saboury Christopher Olumuyiwa Aboluwoye Naghme Sarri-Sarraf

The pH dependence study reveals that the Cys 206 sulphydryl group of bovine carbonicanhydrase in the native form is not exposed. During the reaction of 2,2'-dithiobispyridine (2-DTP) with the enzyme, there was no absorbance change recorded. In the presence ofsurfactants, the pH dependence profiles of the apparent second order rate constants, kapp, forthe reaction of 2-DTP with bovine carbonic a...

Journal: :The Journal of biological chemistry 1996
K Rajaraman B Raman C M Rao

alpha-Crystallin, a multimeric protein, exhibits chaperone-like activity in preventing aggregation of several proteins. We have studied the chaperone-like activity of alpha-crystallin toward heat-induced aggregation of bovine and human carbonic anhydrase. Human carbonic anhydrase aggregates at 60 degrees C, while bovine carbonic anhydrase does not aggregate significantly at this temperature. Re...

Journal: :Biochemical Society transactions 1978
S R Reddy D C Watts

carbonic anhydrase III with an estimated purity of greater than 95%, as judged by electrophoresis in sodium dodecyl sulphate/polyacrylamide gels. Ion-exchange chromatography and salt fractionation were used to purify the bovine carbonic anhydrase 111. Bovine muscle was homogenized and adjusted t o 40% saturation with (NH4)*S04. The supernatant was applied t o a DEAE-cellulose column (2.5cm x 25...

Journal: :Bioorganic & medicinal chemistry letters 2007
Virginija Dudutiene Lina Baranauskiene Daumantas Matulis

A series of benzimidazo[1,2-c][1,2,3]thiadiazole-7-sulfonamides were synthesized and their binding to two carbonic anhydrase isozymes measured by isothermal titration calorimetry (ITC). Human carbonic anhydrase I (hCAI) and bovine carbonic anhydrase II (bCAII) bound the inhibitors with observed association constants in the range from 1.1 x 10(6) to 2.6 x 10(7) M(-1).

Journal: :The Journal of biological chemistry 1977
C Tu D N Silverman

We compare the effect of buffers on the catalysis by bovine carbonic anhydrase, human carbonic anhydrase C (HCA 0, and human carbonic anhydrase B (HCA B) of two types of ‘“0 exchange. Type I, resulting from the hydrationdehydration reaction, is the exchange of IsO between CO, and water. Type II is the exchange of IsO between ‘*Ccontaining and ‘“C-containing species of COZ. Imidazole, 2,4-lutidi...

Journal: :Investigative ophthalmology & visual science 2014
Thomas M Malikowski Jessica B Bosch Sangwon Min Michael E Duffey Sangita P Patel

PURPOSE Carbonic anhydrases play a central buffering role in current models of fluid transport in corneal endothelium, but in humans, clinical use of carbonic anhydrase inhibitors (CAIs) for the management of glaucoma does not cause corneal swelling. This study compares species differences in response to CAIs in human versus bovine corneal endothelial transport. METHODS Short-circuit current ...

Journal: :The Journal of experimental biology 2000
T Peters F Papadopoulos H P Kubis G Gros

The blood serum of the European flounder Platichthys flesus strongly inhibits soluble erythrocytic carbonic anhydrase from the same species. The inhibition is of the uncompetitive type. Hence, the mechanism of the carbonic anhydrase inhibition is different from that of all other known carbonic anhydrase inhibitors. The serum showed no inhibitory effect on carbonic anhydrase from human and bovin...

Journal: :The Journal of biological chemistry 1973
D L Cybulsky S I Kandel M Kandel A G Gornall

Human carbonic anhydrase C and bovine carbonic anhydrase B were modified with the affinity label, bromoacetazolamide, and human carbonic anhydrase B with N-bromoacetylacetazolamide. Tryptic peptides from the modified enzymes, containing alkylated histidines, have been isolated by ion exchange and two-dimensional high voltage electrophoresispaper chromatography. The partial amino acid sequence o...

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