Abstract
Carboxypeptidase Y from bakers’ yeast has been purified in high yields by affinity chromatography. The affinity gel was prepared by coupling the specific inhibitor p-aminobenzylsuccinic acid via an azo linkage to Sepharoseglycyl-tyrosine. This affinity gel was able to bind carboxypeptidase Y specifically and quantitatively from a crude yeast autolysate.
The isolated enzyme appeared homogeneous by gel electrophoresis and ultracentrifugation, while isoelectric focusing revealed the presence of two components with isoelectric points of pH 3.56 and 3.66, respectively. Small differences in amino acid composition and enzymatic properties between the enzyme from danish yeast and the corresponding enzyme isolated from Fleichmann yeast suggested the existence of more than one form of this enzyme.
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Johansen, J.T., Breddam, K. & Ottesen, M. Isolation of carboxypeptidase Y by affinity chromatography. Carlsberg Res. Commun. 41, 1–14 (1976). https://doi.org/10.1007/BF02908689
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DOI: https://doi.org/10.1007/BF02908689