Characterization of a highly glycosylated biosynthetic intermediate of ovalbumin.

Abstract:

:Ovalbumin extracted from oviduct slices incubated with [35S]methionine or [2-3]mannose contained two biosynthetic intermediates, OE and OF (Y. Kato, H. Iwase, and K. Hotta, 1984, J. Biochem. (Tokyo) 95, 455-463). In the present study, these intermediates are further characterized. The 3H dpm/35S dpm ratio of OF labeled with both [35S]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.

journal_name

Arch Biochem Biophys

authors

Kato Y,Iwase H,Hotta K

doi

10.1016/0003-9861(86)90607-7

subject

Has Abstract

pub_date

1986-02-01 00:00:00

pages

408-12

issue

2

eissn

0003-9861

issn

1096-0384

pii

0003-9861(86)90607-7

journal_volume

244

pub_type

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