Immunoaffinity purification and characterization of nucleotide pyrophosphatase from human placenta |
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Authors: | T Yano K Horie R Kanamoto H Kitagawa I Funakoshi I Yamashina |
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Institution: | Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Kyoto University, Japan. |
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Abstract: | Nucleotide pyrophosphatase EC 3.6.1.9] was purified to homogeneity from human placenta using a monoclonal antibody affinity column. By sodium dodecylsulfate--polyacrylamide gel electrophoresis, the purified enzyme showed a major band at a molecular size of 130 K. The enzyme was a glycoprotein with N-linked oligosaccharides consisting of both complex- and oligomannoside-types. Substrate specificity to hydrolyze phosphodiester and phosphosulfate linkages as well as other properties were similar to those of nucleotide pyrophosphatase and phosphodiesterase from other sources. |
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