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Clinical Chemistry 43: 2076-2082, 1997;
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(Clinical Chemistry. 1997;43:2076-2082.)
© 1997 American Association for Clinical Chemistry, Inc.

Articles

Improved purification of human bone sialoprotein and development of a homologous radioimmunoassay

Markus Karmatschek1,a, Ina Maier1, Markus J. Seibel2, Henning W. Woitge2, Reinhard Ziegler2 and Franz P. Armbruster1

1 Immundiagnostik GmbH, Wiesenstr. 4, 64625 Bensheim, Germany.

2 Department of Medicine, Division of Endocrinology and Metabolism, University of Heidelberg Medical School, Bergheimerstr. 58, 69115 Heidelberg, Germany.
a Author for correspondence. Fax Int. +49-6251-39084.

Bone sialoprotein (BSP) is a phosphorylated skeletal glycoprotein. Here we describe a new procedure for the purification of BSP involving wide-pore reversed-phase HPLC, and the development of a homologous RIA for human BSP. The immunoassay showed linearity between 3 and 120 µg/L, a lower detection limit of 0.7 µg/L, and a mean recovery rate of 99.4%. Intraassay variation was 7.0% (mean = 10.9 µg/L) and 6.1% (mean = 38.8 µg/L), and interassay variation was 9.2% (mean = 11.1 µg/L) and 9.4% (mean = 39.0 µg/L). No cross-reactivity was detected with osteocalcin, osteonectin, or bone alkaline phosphatase. Preliminary clinical evaluation in healthy controls (n = 90) showed a mean serum BSP concentration of 12.1 ± 5.0 µg/L (±SD). BSP was significantly increased in patients with Paget disease of bone, primary and secondary hyperparathyroidism, and also in subjects with renal failure without skeletal involvement. Impairment of hepatic function did not affect serum BSP concentrations.




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M. Wuttke, S. Muller, D. P. Nitsche, M. Paulsson, F.-G. Hanisch, and P. Maurer
Structural Characterization of Human Recombinant and Bone-derived Bone Sialoprotein. FUNCTIONAL IMPLICATIONS FOR CELL ATTACHMENT AND HYDROXYAPATITE BINDING
J. Biol. Chem., September 21, 2001; 276(39): 36839 - 36848.
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Copyright © 1997 by the American Association for Clinical Chemistry.