1972
DOI: 10.1016/0005-2795(72)90127-4
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The interaction of some spin-labeled sulfonamides with bovine erythrocyte carbonic anhydrase B

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Cited by 26 publications
(6 citation statements)
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“…2) and resembled the rigid glass, powder or polycrystalline spectrum of the nitroxide radical [7]. This observation indicates that the nitroxide group of sulfonamide I is highly immobilized when this drug binds to the active site of BCA-B [3,7].…”
Section: Resultsmentioning
confidence: 79%
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“…2) and resembled the rigid glass, powder or polycrystalline spectrum of the nitroxide radical [7]. This observation indicates that the nitroxide group of sulfonamide I is highly immobilized when this drug binds to the active site of BCA-B [3,7].…”
Section: Resultsmentioning
confidence: 79%
“…The large central peak in figure 2 con tains contributions from both unbound and bound sulfonamide I. Since peak B in figure 2 contains little or no contribution from the broad spec trum of the highly immobilized enzyme-bound sulfonamide I [3], the amplitude of this peak can serve as a measure of free sulfonamide I in the system. The association constant of sulfonamide I for BCA-B was esti mated from measurements of the amplitude of peak B to be 6.25 x 10° M_1.…”
Section: Resultsmentioning
confidence: 99%
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“…The distance corresponding to this break has been interpreted as the minimum depth of the cleft [13,14]. The essential sulfhydryl group of chicken liver Fru-Pzase is therefore most likely located in a cleft-like environment of 10.5 A in depth.…”
Section: Modification Of the Enzyme By Nitroxidecontaining Iodoacetammentioning
confidence: 99%