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J. Biochem, 1984, Vol. 96, No. 4 937-947
© 1984 Japanese Biochemical Society

research-article

Characterization, Purification, and SubceUuIar Localization of Bovine Thyroid Sialidases1

Guido Van DESSEL*, Marc De WOLF**, Albert LAGROU**, Herwig HILDERSON** and Wilfried DIERICK*,**,2

*UIA-Laboratory of Pathological Biochemistry
**RUCA-Laboratory of Human Biochemistry, University of Antwerp Groenenborgerlaan 171 B2020 Antwerp, Belgium

2To whom correspondence should be addressed.

Sialidase activities have been studied in bovine thyroid using sialoglycolipids, sialoglycoproteins, sialo-oligosaccharides and fluorogenic 4-methylumbelliferyl{alpha}-D-N- acetylneuraminate as substrates. No sialidase activity could be detected towards native glycoprotein substrates. From enzme kinetics, effector data and more convincingly from subcellular studies in became clear that in bovine thyroid at least two sialidase activities were present, a sialyllactitol sialidase confined to the lysosomal membrane and a glycolipid sialidase residing in the plasma membrane and displaying the features of a true ectoenzyme. The lipid requirement for full enzyme activity supported the membrane bound character of both sialidase activities. A soluble sialidase activity could not be demonstrated. After solubilization by CHAPS treatment, partial purification of the sialyllactitol sialidase could be achieved by affinity chromatography (Sepharose diamino dipropylamino-N-acetyleuraminic acid). The purified enzyme was extremely labile. Titration of the sialidase preparation with amino acid modifying gents revealed that sulfhydryl- and typtophanyl groups were essential for the silaidase action.

1This work was supported in part by Belgian FGWO grant n° 3.0057.81 by NIH grant 1RO1 AM32136–01 by a grant from the Roland family.


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