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Sodium borohydride reduces selectively two disulfide bonds in trypsinogen and trypsin which are nonessential for activity. Chymotrypsinogen and chymotrypsin are not reduced under these conditions. The disulfide which is modified in trypsinogen is located in a homologous position in chymotrypsinogen which suggests that the two proteins differ in conformation in this region.
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Light et al. (1967) studied this question.
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