| dc.contributor.author |
Gotschall, R. Russell |
en_US |
| dc.contributor.author |
Bousfield, George R. |
en_US |
| dc.date.accessioned |
2012-01-24T17:48:34Z |
|
| dc.date.available |
2012-01-24T17:48:34Z |
|
| dc.date.issued |
1996-06 |
en_US |
| dc.identifier |
8641208 |
en_US |
| dc.identifier |
HD-29047 |
en_US |
| dc.identifier |
0375040 |
en_US |
| dc.identifier.citation |
Endocrinology. 1996 Jun; 137(6): 2543-57. |
en_US |
| dc.identifier.issn |
0013-7227 |
en_US |
| dc.identifier.uri |
http://dx.doi.org/10.1210/en.137.6.2543 |
|
| dc.identifier.uri |
http://hdl.handle.net/10057/4131 |
|
| dc.description |
Click on the DOI link below to access the article (may not be free). |
en_US |
| dc.description.abstract |
Equine gonadotropin alpha-subunit glycosylation was examined by releasing oligosaccharides using a sequential enzymatic deglycosylation protocol and comparing the released oligosaccharide populations using a high resolution oligosaccharide mapping technique. Digestion of native alpha-subunit preparations with peptide-N-glycosidase altered their mobilities during SDS-PAGE under reducing conditions to positions intermediate between the corresponding native alpha-subunit and completely deglycosylated alpha-subunit bands. Complete alpha-subunit deglycosylation required reduction of disulfide bonds. Results of solid-phase Edman degradation demonstrated that partial deglycosylation occurred exclusively at Asn56. Oligosaccharide mapping of total oligosaccharides obtained by enzymatic deglycosylation of reduced, carboxymethylated alpha-subunit preparations revealed hormone-specific patterns of glycosylation in eLH alpha and eCG alpha. Oligosaccharide mapping of individual glycosylation sites revealed that hormone-specific glycosylation was primarily restricted to Asn56 of both subunit preparations and revealed a hormone-specific pattern of Asn56 glycosylation in eFSH alpha that was obscured in the total oligosaccharide map. eLH alpha Asn56 oligosaccharides appeared to be primarily seven variants of a monoantennary structure. eCG alpha Asn56 oligosaccharides consisted of one of two forms, either a sialylated biantennary oligosaccharide that appeared identical to a commercial carbohydrate standard or a lactosamine variant of that structure. |
en_US |
| dc.description.sponsorship |
NICHD NIH HHS |
en_US |
| dc.language.iso |
eng |
en_US |
| dc.publisher |
The Endocrine Society |
en_US |
| dc.relation.ispartofseries |
Endocrinology |
en_US |
| dc.source |
NLM |
en_US |
| dc.subject |
Research Support, U.S. Gov't, P.H.S. |
en_US |
| dc.subject.mesh |
Amidohydrolases/metabolism |
en_US |
| dc.subject.mesh |
Amino Acid Sequence |
en_US |
| dc.subject.mesh |
Animals |
en_US |
| dc.subject.mesh |
Asparagine/chemistry |
en_US |
| dc.subject.mesh |
Cyanogen Bromide |
en_US |
| dc.subject.mesh |
Disulfides/chemistry |
en_US |
| dc.subject.mesh |
Electrophoresis, Polyacrylamide Gel |
en_US |
| dc.subject.mesh |
Glycoprotein Hormones, alpha Subunit/metabolism |
en_US |
| dc.subject.mesh |
Glycosylation |
en_US |
| dc.subject.mesh |
Horses |
en_US |
| dc.subject.mesh |
Molecular Sequence Data |
en_US |
| dc.subject.mesh |
Oligosaccharides/metabolism |
en_US |
| dc.subject.mesh |
Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase |
en_US |
| dc.subject.mesh |
Glycoprotein Hormones, alpha Subunit/chemistry |
en_US |
| dc.subject.mesh |
Oligosaccharides/chemistry |
en_US |
| dc.title |
Oligosaccharide mapping reveals hormone-specific glycosylation patterns on equine gonadotropin alpha-subunit Asn56 |
en_US |
| dc.type |
Article |
en_US |
| dc.description.version |
peer reviewed |
en_US |