Abstract
Summary The objective of this research was to purify the protein that binds and reduces the activity of potato (Solanum tuberosum L.) tuber acid invertase. Our attempt to isolate invertase inhibitor from potatoes (cv. Katahdin) using previously published procedures resulted in the inhibitor co-purifying with several other proteins without inhibitor function, of similar weight but different pI values. These impurities were obscured on SDS-PAGE discontinuous polyacrylamide gels since after the first purification step all the proteins had molecular weights ranging from 17 to 18 kDa. Using a glycerol-propyl silane (GPS-) modified silica column in combination with a Tricine buffer, a single protein band was identified as the inhibitor on IEF-PAGE gels. The inhibitor was identified as a protein that has a mol. wt of approximately 17 and a pI of 5.1.
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