ARTICLE

ISOLATION OF RAT LIVER PLASMA MEMBRANES : Use of Nucleotide Pyrophosphatase and Phosphodiesterase I as Marker Enzymes

Oscar Touster ¹, N. N. Aronson Jr. ¹, John T. Dulaney ¹, and Herman Hendrickson ¹

¹ From the Department of Molecular Biology, Vanderbilt University, Nashville, Tennessee 37203.

Dr. Aronson's present address is the Department of Biochemistry, Frear Laboratories, Pennsylvania State University, University Park, Pennsylvania 16802, and Dr. Hendrickson's present address is the Department of Neurology, University of Miami Medical School, Miami, Florida 33124.

Nucleotide pyrophosphatase and phosphodiesterase I of rat liver have been found to be localized primarily in cell particulates highly enriched with respect to the most commonly accepted plasma membrane marker, 5'-nucleotidase, and therefore should themselves be assigned a plasma membrane localization. The observation that plasma membranes sediment in isotonic sucrose with both nuclear and microsomal fractions was exploited to obtain plasma membrane preparations from each fraction. Both preparations are similar in chemical and enzymic composition. Moreover, the preparative method developed in this study appears to give the best combination of yield, purity, and reproducibility available. The question of the possible identity of nucleotide pyrophosphatase and phosphodiesterase I is considered, and evidence is presented suggesting that these activities may be manifestations of the same enzyme.

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