Immunoaffinity purification and characterization of nucleotide pyrophosphatase from human placenta.
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.
Yano
T
T
Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Kyoto University, Japan.
Horie
K
K
Kanamoto
R
R
Kitagawa
H
H
Funakoshi
I
I
Yamashina
I
I
D000596:Amino Acids / Q000032:analysis; D000911:Antibodies, Monoclonal; D002241:Carbohydrates / Q000032:analysis; D002846:Chromatography, Affinity; D006023:Glycoproteins / Q000302:isolation & purification*; D006801:Humans; D008970:Molecular Weight; D010920:Placenta / Q000201:enzymology*; D011755:Pyrophosphatases / Q000302:isolation & purification* / Q000378:metabolism; D013379:Substrate Specificity
D000596:Amino Acids; D000911:Antibodies, Monoclonal; D002241:Carbohydrates; D006023:Glycoproteins; D011755:Pyrophosphatases; C021899:nucleotide pyrophosphatase