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PMID: 6273593 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

The dynamic state of liver gap junctions.

Journal of supramolecular structure and cellular biochemistry ·Vol. 16 ·No. 3 ·1981-00-00 ·Pages 221-32

Yancey SB, Nicholson BJ, Revel JP

Abstract

By the use of a simple, rapid method for the isolation of gap junctions from small amounts of rat liver (2-3 g), we have followed the incorporation of the radiolabeled amino acid precursors 3H-leucine and 35S-methionine into the gap junction protein. In timed studies with 35S-methionine as precursor, the specific activity in the protein is maximal by 4 h after a single injection of 300 microCi/100 g body weight. From the decay in the specific activity with time after a single injection, the gap junction protein has an apparent half-life of about 19 h. Because of problems of reutilization of radiolabeled amino acid with 35S-methionine as precursor, this apparent half-life probably overestimates the true half-life and indicates a surprisingly rapid turnover of the gap junction protein. This short half-life suggests that, in rat liver, the gap junctions may be very responsive to alterations in physiological demands.

MeSH Terms
Animals Cell Fractionation Connexins Half-Life Intercellular Junctions/ultrastructure Kinetics Liver/ultrastructure Membrane Proteins/metabolism Peptide Fragments/analysis Rats Rats, Inbred Strains
Chemicals
Connexins Membrane Proteins Peptide Fragments
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Yancey S B
Nicholson B J
Revel J P
Article Info
Journal
Journal of supramolecular structure and cellular biochemistry
Abbr.
J Supramol Struct Cell Biochem
ISSN
0275-3723
Published
1981-00-00
Pages
221-32
Language
English
Region
United States
NLM ID
8106911
Subset
IM
Grants
NIGMS NIH HHS · GM 06965 · United States
NCRR NIH HHS · RR 07003 · United States
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