Presence of an endo-beta-galactosidase degrading the linkage region between the chondroitin sulfate chain and core peptide of proteoglycan

Biochemical and Biophysical Research Communications
K TakagakiMasahiko Endo

Abstract

Pyridylamino chondroitin sulfate, of which the reducing terminal xylose was coupled with a fluorescent 2-aminopyridine, was incubated at pH 4.0 with an extract from the mid-gut gland of Patnopecten. The high- and low-molecular-weight products were separated by ethanol precipitation, and identified by high-performance liquid chromatography analysis. The enzyme was found to expose a galactose residue at the reducing terminus of chondroitin sulfate, and also released the pyridylamino disaccharide, galactosylxylose, from the reducing terminal site of pyridylamino chondroitin sulfate. These results suggest that endo-beta-galactosidase activity, which hydrolyzes the galactosylgalactose linkage of peptidochondroitin sulfate, is present in the mid-gut gland of Patnopecten.

References

Jan 1, 1979·Journal of Biochemistry·S HaseY Matsushima
Mar 19, 1987·Biochimica Et Biophysica Acta·H Matsue, M Endo
Jan 1, 1986·Annual Review of Biochemistry·J R HassellV C Hascall

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Citations

Aug 2, 2012·Proceedings of the Japan Academy. Series B, Physical and Biological Sciences·Masahiko Endo, Ikuko Kakizaki
Mar 9, 2011·Journal of Pharmaceutical and Biomedical Analysis·Keita Yamada, Kazuaki Kakehi
Jun 23, 2005·Matrix Biology : Journal of the International Society for Matrix Biology·Peter J RoughleyJohn S Mort
Feb 12, 2008·Current Protocols in Molecular Biology·M N Fukuda
Nov 15, 1990·Analytical Biochemistry·T NakamuraM Endo
Oct 15, 1990·Biochemical and Biophysical Research Communications·T NakamuraM Endo

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