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Title: Crystallization and X-ray investigation of vitamin D-binding protein from human serum. Identification of the crystal content
Authors: Verboven, C C ×
De Bondt, H L
De Ranter, Camiel
Bouillon, Roger
Van Baelen, Hugo #
Issue Date: Jul-1995
Publisher: Pergamon-elsevier science ltd
Series Title: The Journal of steroid biochemistry and molecular biology vol:54 issue:1-2 pages:11-4
Abstract: Vitamin D-binding protein (DBP), a multifunctional, highly polymorphic glycoprotein responsible for the transport of vitamin D and for sequestering extracellular actin, was isolated from human serum and crystallized using vapour diffusion methods. The crystals were grown from 7.5% v/v polyethylene glycol 400 and 0.1 M acetate buffer at pH 4.6. These crystals show diffraction patterns consistent with the tetragonal space groups P4(1) and P4(3) with unit cell dimensions a = b = 135.5(4) A and c = 75.9(4) A. They diffract to 2.3 A. Using polyacrylamide gel electrophoresis it was shown that according to their electrophoretic mobility the O-glycosylated isoforms, with a terminal sialic acid residue, are absent in the crystals.
URI: 
ISSN: 0960-0760
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Clinical and Experimental Endocrinology
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× corresponding author
# (joint) last author

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