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 Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

We have isolated a cDNA containing the complete coding sequence of bovine liver phosphatidylcholine transfer protein (PC-TP). The deduced amino acid sequence consists of 213 amino acid residues and is, except for a lysine instead of an arginine at position 167, identical to the sequence determined by Edman degradation [Akeroyd, Moonen, Westerman, Puyk and Wirtz (1981) Eur. J. Biochem. 114, 385-391]. A cDNA encoding amino acid residues 41-214 of mouse lung PC-TP was also isolated. The predicted amino acid sequence was 90% similar (81% identical) to the corresponding sequence of bovine liver PC-TP, demonstrating that PC-TP is conserved among mammalian species. By Southern blot analysis, evidence was obtained for the presence of a single bovine PC-TP-encoding gene. The expression of the PC-TP gene was determined during mouse embryonic development and in adult mouse tissues using an RNase protection assay. PC-TP RNA was present in embryos at all stages of development as early as the embryonic stem cell, suggesting a role for PC-TP in cell growth and differentiation. Towards the end of embryonic development, just before term, high levels of PC-TP RNA were found in the liver. This level was even higher 7 days post-term. In addition to adult liver, high levels of PC-TP RNA were also found in kidney and testis. The prominent presence of PC-TP in developing and adult liver is compatible with its proposed role in bile formation.

cDNA cloning and tissue-specific expression of the phosphatidylcholine transfer protein gene