Abstract
The modification of amino groups in Taka-amylase A (TAA) using trinitrobenzene sulfonic acid (TNBS), formaldehyde, and pyridoxal 5'-phosphate (PLP) was compared with that using a fluorescent reagent, ο-phthalaldehyde (OPA). Although OPA resulted in potent inactivation of TAA as described in previous papers, the other three reagents described above caused no such inactivation of TAA. HPLC analysis showed that reactions of OPA with Lys residue differed greatly depending on the pH and the presence of Cys residue. Therefore, the different response of TAA for the modifications between OPA and other reagents suggested that Cys residue played an important role in the OPA reaction.
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