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Presence of Ornithine in the Urate-binding α1—2Globulin

Nature New Biology volume 231, pages 118–119 (1971)Cite this article

Abstract

THE urate-binding α1–α2 globulin has been isolated from human plasma in a highly purified state1. The protein was purified by DEAE-‘Sephadex’, ammonium sulphate precipitation and semi-preparative Polyacrylamide gel electrophoresis. The urate-binding α1–α2 globulin is a rod-shaped glycoprotein, containing 12.1% carbohydrate, with an isoelectric point of 4.6 and a molecular weight of 67,000 ± 4,000. Amino-acid analysis indicated an unknown basic compound which appeared as an extra peak just in front of lysine1. To identify this compound, high voltage paper electrophoresis has been carried out on a plate electrophoresis apparatus in pyridine-acetate buffer pH 3.5. A spot separated out corresponding to ornithine. Amino-acid analysis on a BC-200 automatic analyser (Bio-Cal Instruments Co., West Germany), with a 54 cm column at 55° C and with 0.35 M sodium citrate buffer, pH 5.28, as elution buffer at a flow-rate of 150 ml./h, showed that ornithine was present. The presence of ornithine in the protein hydrolysate was also verified by gas chromatography/mass spectrometry2.

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References

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Authors and Affiliations

  1. Department of Biochemistry, University of Oslo, Blindern

    K. SLETTEN & I. AAKESSON

  2. Oslo City Hospital, Ullevaal, Department VII, Oslo

    J. O. ALVSAKER

Authors
  1. K. SLETTEN
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  2. I. AAKESSON
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  3. J. O. ALVSAKER
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SLETTEN, K., AAKESSON, I. & ALVSAKER, J. Presence of Ornithine in the Urate-binding α1—2Globulin. Nature New Biology 231, 118–119 (1971). https://doi.org/10.1038/newbio231118a0

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