A GM2-specific beta-hexosaminidase from the roe of striped mullet (Mugil cephalus).
J Biol Chem
; 263(3): 1325-8, 1988 Jan 25.
Article
in En
| MEDLINE
| ID: mdl-2961751
ABSTRACT
The roe of striped mullet (Mugil cephalus) was found to contain a beta-hexosaminidase different from the beta-hexosaminidases isolated from other sources. The enzyme from mullet roe is able to cleave GalNAc from GM2 without the assistance of either an activator protein or a detergent. It also cleaves the oligosaccharide derived from GM2 and other oligosaccharides containing the GM2 sequence GalNAc beta 4(NeuAc alpha 3)Gal-. However, it is not effective in hydrolyzing neutral glycosphingolipids containing terminal GalNAc or GlcNAc, such as GbOse4Cer, GgOse3Cer, or LcOse3Cer. These results indicate that mullet roe beta-hexosaminidase can specifically cleave GalNAc from the glycoconjugates containing the GM2 sequence. No beta-hexosaminidase with such specificity has been previously described. Thus, this unique enzyme should be very useful for the detection and analysis of glycoconjugates containing the oligosaccharide chains with GM2 sequence.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Beta-N-Acetylhexosaminidases
/
Fishes
/
G(M2) Ganglioside
/
Gangliosides
Limits:
Animals
Language:
En
Journal:
J Biol Chem
Year:
1988
Document type:
Article