English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

A phosphorylated protein with molecular mass of 25,000 (pp25), a new vitellogenin gene product [Yoshitome, S. et al., unpublished results], was shown to be phosphorylated on Ser-4 by protein kinase C [Hashimoto, E. et al.(1996) J. Biochem. 119, 626-632]. In order to examine the in vivo phosphorylation of this site, an anti-phosphopeptide antibody was prepared and used for qualitative and quantitative analyses. This antibody specifically recognized the Ser-4-phosphorylated pp25 and did not react with Ser-4-dephosphorylated pp25. About 18% of pp25 in the cytosolic fraction was phosphorylated in vivo. The migration of pp25 in SDS-PAGE was increased and the proteolysis of this protein by trypsin or α-chymotrypsin was influenced by introduction of phosphate at this site. During oocyte maturation and initial stages of embryogenesis, the changes in intensity of the immunostained pp25 bands reacted with this antibody were parallel with those detected by an anti-peptide antibody recognizing all forms of pp25. These results indicate that the phosphorylation of Ser-4 actually occurs in oocytes and seems to be related to the structural change of this protein although its involvement in the functional change is not clear at this time.

biomedical research

Studies on the Phosphorylation of Ser-4 in Mr 25,000 Protein, a New Vitellogenin Gene Product Detected in Xenopas laevir Oocytes, Using Anti-phosphopeptide Antibody against this Site