Abstract
ESSENTIAL thiol groups of enzymes are usually detected by the inactivation of the enzyme with sulphydryl reagents, such as substances forming mercaptide, or oxidizing or alkylating substances1. Yeast carboxylase seems to be affected in a rather uneven and contradictory way by sulphydryl group detectors since 4-aminophenyldichloroarsine2, p-chloromercuribenzoate3, iodine3, iodoacetate3, cupric3,4, mercuric and silver ions4, or quinone5 inhibit the enzyme, while in other experiments, lewisite oxide6, ethylarsenoxide7, iodoacetate4 or ethyl iodoacetate8 do not modify its activity significantly. It must be pointed out: (a) that inhibition by a single thiol reagent does not prove the existence of sulphydryls, since even very selective mercurial compounds9 can inactivate enzymes which by other evidence do not seem to contain essential thiol groups; and (b) that the effect of sulphydryl detectors often depends on the purity of the enzyme preparation tested10, a circumstance neglected in some of the work quoted. Therefore, considering the essential part played by thiol groups in most of the enzymes related to pyruvate metabolism2, it seemed interesting to make a systematic study of the action of several types of thiol reagents on a conveniently purified carboxylase, and for that purpose we have used the preparation described by Green et al.4 ( about 12,000).
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STOPPANI, A., ACTIS, A., DEFERRARI, J. et al. Essential Role of Thiol Groups in Carboxylase. Nature 170, 842–843 (1952). https://doi.org/10.1038/170842a0
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DOI: https://doi.org/10.1038/170842a0
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