Purification of guinea pig liver transglutaminase using a phenylalanine-sepharose 4B affinity column |
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Authors: | P P Brookhart P L McMahon M Takahashi |
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Affiliation: | Department of Physiology and Biophysics, Rutgers Medical School, Piscataway, New Jersey 08854 USA |
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Abstract: | Guinea pig liver transglutaminase has been purified utilizing an improved protocol. The new steps include QAE-Sephadex ion-exchange, hydroxylapatite adsorption, and affinity chromatography using a phenylalanine-Sepharose column. The overall yield for the enzyme was 31%. This new scheme should enable more laboratories to take advantage of the protein crosslinking and labeling properties of transglutaminase. |
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Keywords: | To whom all correspondence should be addressed. |
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