PMID: 2125279Dec 17, 1990Paper

Photoaffinity labeling of the lysosomal neuraminidase from bovine testis

FEBS Letters
G T van der HorstF W Verheijen

Abstract

ASA-NeuAc2en, a photoreactive arylazide derivative of sialic acid, is shown to be a powerful competitive inhibitor of lysosomal neuraminidase from bovine testis (Ki approximately 21 microM). Photoaffinity labeling and partial purification of preparations containing this lysosomal neuraminidase activity result in specifically and non-specifically labeled polypeptides. Only labeling in a 55 kDa polypeptide is found to be specific, since it could be prevented by the competitive neuraminidase inhibitor NeuAc2en. We conclude that the 55 kDa polypeptide in the bovine testis beta-galactosidase/neuraminidase/protective protein complex contains the catalytic site of neuraminidase.

References

May 30, 1978·Biochemical and Biophysical Research Communications·D A WengerC Wharton
Jan 24, 1977·Biochemical and Biophysical Research Communications·M CantzJ Spranger
Jan 2, 1987·European Journal of Biochemistry·F W VerheijenH Galjaard
Aug 1, 1982·Proceedings of the National Academy of Sciences of the United States of America·A D'AzzoH Galjaard
Sep 30, 1982·Biochemical and Biophysical Research Communications·F VerheijenH Galjaard

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Citations

Feb 22, 1994·Biochimica Et Biophysica Acta·Y Okamura-OhoJ W Callahan
May 24, 2008·Glycobiology·Brian P Rempel, Stephen G Withers
Aug 8, 2014·Chemistry : a European Journal·Lianne I WillemsHermen S Overkleeft

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