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J Biol Chem, Vol. 274, Issue 4, 2456-2463, January 22, 1999
, and
From the Department of Life Science, Aichi University of Education,
Aichi 448-8542, Japan and Chondroitin 4-sulfotransferase, which transfers
sulfate from 3'-phosphoadenosine 5'-phosphosulfate to position 4 of
N-acetylgalactosamine in chondroitin, was purified
1900-fold to apparent homogeneity with 6.1% yield from the serum-free
culture medium of rat chondrosarcoma cells by affinity chromatography
on heparin-Sepharose CL-6B, Matrex gel red A-agarose,
3',5'-ADP-agarose, and the second heparin-Sepharose CL-6B.
SDS-polyacrylamide gel electrophoresis of the purified enzyme showed
two protein bands. Molecular masses of these protein were 60 and 64 kDa
under reducing conditions and 50 and 54 kDa under nonreducing
conditions. Both the protein bands coeluted with chondroitin
4-sulfotransferase activity from Toyopearl HW-55 around the position of
50 kDa, indicating that the active form of chondroitin
4-sulfotransferase is a monomer. Dithiothreitol activated the purified
chondroitin 4-sulfotransferase. The purified enzyme transferred sulfate
to chondroitin and desulfated dermatan sulfate. Chondroitin sulfate A
and chondroitin sulfate C were poor acceptors. Chondroitin sulfate E
from squid cartilage, dermatan sulfate, heparan sulfate, and completely
desulfated N-resulfated heparin hardly served as acceptors of the
sulfotransferase. The transfer of sulfate to the desulfated dermatan
sulfate occurred preferentially at position 4 of the
N-acetylgalactosamine residues flanked with glucuronic acid
residues on both reducing and nonreducing sides.
Bone and Joint Center, Henry
Ford Hospital, Detroit, Michigan 48202
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