Kinetic Product Analysis of Aspartyl Proteinases Utilizing New Synthetic Substrates and Reversed Phase HPLC
Kinetic characterization of the Aspartyl Proteinase family of enzymes has been hampered by the lack of convenient substrates. The enzymatic preference for cleavage between two hydrophobic residues causes most small synthetic substrates to be very insoluble in aqueous buffers. Since these enzymes do not cleave terminal residues readily, p-nitroanilides or p-nitrophenyl esters are not useful as chromophoric substrates and most previous assays required measurement of newly generated amino termini with ninhydrin or fluorescamine.
KeywordsAspartic Proteinase Synthetic Substrate HPLC Grade Methanol Aspartyl Proteinase Phenyl Ester
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