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Site-specific and complete enzymic deglycosylation of the native human chorionic gonadotropin alpha-subunit.
- Source :
-
European journal of biochemistry [Eur J Biochem] 1995 Aug 01; Vol. 231 (3), pp. 754-60. - Publication Year :
- 1995
-
Abstract
- Numerous studies have shown that glycosylation of the alpha-subunit of human chorionic gonadotropin (alpha hCG) is essential for the biological activity of this hormone. To obtain detailed insight into the function of N-glycosylation, the availability of site-specifically and fully deglycosylated alpha-subunits obtained under non-denaturing conditions is a prerequisite. NMR spectroscopy in combination with FAB-mapping demonstrates that only Asn52 of the alpha-subunit is accessible to digestion by peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase F under native conditions. Treatment of native alpha hCG with endo-beta-N-acetylglucosaminidase B results in full deglycosylation yielding alpha hCG with one GlcNAc residue at both Asn52 and Asn78.
- Subjects :
- Amidohydrolases metabolism
Amino Acid Sequence
Carbohydrate Sequence
Glycosylation
Humans
Magnetic Resonance Spectroscopy
Molecular Sequence Data
Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
Spectrometry, Mass, Fast Atom Bombardment
Glycoprotein Hormones, alpha Subunit metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0014-2956
- Volume :
- 231
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- European journal of biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 7544284
- Full Text :
- https://doi.org/10.1111/j.1432-1033.1995.tb20758.x