Characterization of a highly glycosylated biosynthetic intermediate of ovalbumin
| ISSN: |
0003-9861
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|---|---|
| Source: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
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| Topics: |
Biology
Chemistry and Pharmacology
Physics
|
| Type of Medium: |
Electronic Resource
|
| URL: |
| _version_ | 1798292194408267776 |
|---|---|
| autor | Kato, Y. Iwase, H. Hotta, K. |
| autorsonst | Kato, Y. Iwase, H. Hotta, K. |
| book_url | http://dx.doi.org/10.1016/0003-9861(86)90607-7 |
| datenlieferant | nat_lic_papers |
| fussnote | Ovalbumin extracted from oviduct slices incubated with [^3^5S]methionine or [2-^3]mannose contained two biosynthetic intermediates, OE and OF (). In the present study, these intermediates are further characterized. The ^3H dpm^3^5S dpm ratio of OF labeled with both [^3^5S]methionine and [^3H]mannose was twice that or greater than that of OE. The tritium-labeled OF migrated more slowly than OE on sodium dodecyl sulfate-gel electrophoresis and had a molecular weight exceeding that of OE by about 1500. These findings, along with the fact that [^3H]OF had sugar chains similar to those of [^3H]OE, suggest that OF may possibly have two sugar chains in one molecule. For confirmation of this, the glycosylation sites of OF were examined. Peptic and tryptic glycopeptides were prepared from [2-^3H]mannose-labeled OF and the other ovalbumin subfractions-OA, OC, OD, and OE-and then analyzed by high-performance liquid chromatography. The peptic glycopeptides prepared from [^3H]OF contained glycopeptides in addition to those derived from the other subfractions although tryptic glycopeptides obtained from [^3H]OF were similar to those from the other subfractions. This shows that the above hypothesis is valid. |
| hauptsatz | hsatz_simple |
| identnr | NLZ183420713 |
| issn | 0003-9861 |
| journal_name | Archives of Biochemistry and Biophysics |
| materialart | 1 |
| package_name | Elsevier |
| publikationsort | Amsterdam |
| publisher | Elsevier |
| reference | 244 (1986), S. 408-412 |
| search_space | articles |
| shingle_author_1 | Kato, Y. Iwase, H. Hotta, K. |
| shingle_author_2 | Kato, Y. Iwase, H. Hotta, K. |
| shingle_author_3 | Kato, Y. Iwase, H. Hotta, K. |
| shingle_author_4 | Kato, Y. Iwase, H. Hotta, K. |
| shingle_catch_all_1 | Kato, Y. Iwase, H. Hotta, K. Characterization of a highly glycosylated biosynthetic intermediate of ovalbumin 0003-9861 00039861 Elsevier |
| shingle_catch_all_2 | Kato, Y. Iwase, H. Hotta, K. Characterization of a highly glycosylated biosynthetic intermediate of ovalbumin 0003-9861 00039861 Elsevier |
| shingle_catch_all_3 | Kato, Y. Iwase, H. Hotta, K. Characterization of a highly glycosylated biosynthetic intermediate of ovalbumin 0003-9861 00039861 Elsevier |
| shingle_catch_all_4 | Kato, Y. Iwase, H. Hotta, K. Characterization of a highly glycosylated biosynthetic intermediate of ovalbumin 0003-9861 00039861 Elsevier |
| shingle_title_1 | Characterization of a highly glycosylated biosynthetic intermediate of ovalbumin |
| shingle_title_2 | Characterization of a highly glycosylated biosynthetic intermediate of ovalbumin |
| shingle_title_3 | Characterization of a highly glycosylated biosynthetic intermediate of ovalbumin |
| shingle_title_4 | Characterization of a highly glycosylated biosynthetic intermediate of ovalbumin |
| sigel_instance_filter | dkfz geomar wilbert ipn albert fhp |
| source_archive | Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
| timestamp | 2024-05-06T08:44:38.534Z |
| titel | Characterization of a highly glycosylated biosynthetic intermediate of ovalbumin |
| titel_suche | Characterization of a highly glycosylated biosynthetic intermediate of ovalbumin Ovalbumin extracted from oviduct slices incubated with [^3^5S]methionine or [2-^3]mannose contained two biosynthetic intermediates, OE and OF (). In the present study, these intermediates are further characterized. The ^3H dpm^3^5S dpm ratio of OF labeled with both [^3^5S]methionine and [^3H]mannose was twice that or greater than that of OE. The tritium-labeled OF migrated more slowly than OE on sodium dodecyl sulfate-gel electrophoresis and had a molecular weight exceeding that of OE by about 1500. These findings, along with the fact that [^3H]OF had sugar chains similar to those of [^3H]OE, suggest that OF may possibly have two sugar chains in one molecule. For confirmation of this, the glycosylation sites of OF were examined. Peptic and tryptic glycopeptides were prepared from [2-^3H]mannose-labeled OF and the other ovalbumin subfractions-OA, OC, OD, and OE-and then analyzed by high-performance liquid chromatography. The peptic glycopeptides prepared from [^3H]OF contained glycopeptides in addition to those derived from the other subfractions although tryptic glycopeptides obtained from [^3H]OF were similar to those from the other subfractions. This shows that the above hypothesis is valid. |
| topic | W V U |
| uid | nat_lic_papers_NLZ183420713 |