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09:54
Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
Published on: December 26, 2011
An endogalactosaminidase from Streptomyces griseus
Canadian Journal of Biochemistry
|December 1, 1975
Summary
A novel endogalactosaminidase enzyme from Streptomyces griseus was purified. This enzyme cleaves specific galactosamine linkages, aiding in the release of Neurospora sporelings from surfaces.
Area of Science:
- Microbiology
- Biochemistry
- Enzymology
Background:
- Oligogalactosaminoglycans are galactosamine-rich oligosaccharides found in microbial culture filtrates.
- Neurospora sporelings are observed to be anchored to surfaces by galactosaminoglycan molecules.
Purpose of the Study:
- To purify and characterize an enzyme capable of cleaving galactosamine linkages.
- To investigate the role of galactosaminoglycan in anchoring Neurospora sporelings.
Main Methods:
- Purification of endogalactosaminidase from Streptomyces griseus culture filtrate.
- Enzyme activity assays on oligogalactosaminoglycan and galactosaminoglycan.
- Chromatographic separation (DEAE-cellulose) to correlate enzyme activity with sporeling release.
Main Results:
- A 34-fold purified endogalactosaminidase was obtained, tentatively identified as an endo-alpha-(1 leads to 4)-galactosaminidase.
- The enzyme specifically cleaved GalN-GalN linkages in oligogalactosaminoglycan but was inactive against N-acetyl-oligogalactosaminoglycan and chitosan.
- The enzyme degraded high molecular weight galactosaminoglycan and released anchored Neurospora sporelings, with both activities co-eluting during purification.
Conclusions:
- The purified endogalactosaminidase plays a role in breaking down galactosaminoglycans.
- The findings support the hypothesis that galactosaminoglycan mediates the attachment of Neurospora sporelings to surfaces.
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