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A factor that activates oscillatory chloride currents in Xenopus oocytes copurifies with a subfraction of serum albumin. by G. Tigyi; A. Henschen; R. Miledi is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Vertebrate blood sera contain a factor that elicits oscillatory chloride currents in Xenopus oocytes through activation of the phosphatidylinositol second messenger system. This factor was purified from rabbit and human sera by a sequence of Blue-Agarose chromatography, concanavalin A affinity chromatography, and hydroxyapatite fractionation, yielding a single active protein band (67 kDa). This protein is a subfraction of serum albumin, as revealed by its molecular mass, isoelectric properties, peptide maps, amino acid composition, and NH2-terminal sequence. Moreover, the factor could be purified with a monoclonal antibody to serum albumin and its ability to elicit oscillatory currents was inhibited by several polyclonal-monospecific antibodies to serum albumin. Various commercial high purity albumin preparations elicited oscillatory currents in oocytes. The activity of albumin was partially reduced by charcoal absorption and was greatly diminished when crystalline albumin was extracted with dry methanol. However, the activity was resistant to extraction with chloroform/ether, disulfide cleavage, and denaturation with 8 M urea, 6 M guanidinium chloride, and 1% sodium dodecyl sulfat

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Author

G. Tigyi; A. Henschen; R. Miledi

Publisher

Elsevier BV

Published

1991

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)