TY - JOUR
T1 - Comparative analysis of the gap junction protein from rat heart and liver
T2 - Is there a tissue specificity of gap junctions?
AU - Gros, Daniel B.
AU - Nicholson, Bruce J.
AU - Revel, Jean Paul
N1 - Funding Information:
We wash to thank Mrs. Jean Edens and Mr. Pat Koen for their very valuable help in electron microscopy, as well as Ms. Renee Thorf and Susan Mangrum for the preparation of the manuscript. Bacteriorhodopsin was a gift from Dr. J. Horwitz, UCLA Medical School. The research was supported by Research Grant GM 06965 and Biomedical Research Support Program RR 07003 from the National Institutes of Health as well as a Ross Foundation FellowshIp awarded to B. J. N. D. B. G. was a recipient of grants from NATO and the Fondatton pour la Recherche Medicale.
PY - 1983/12
Y1 - 1983/12
N2 - Gap junctions have been isolated from both rat heart and liver, tissues where junctions are typical in appearance and physiology. The purity of the fractions obtained was monitored by electron microscopy (thin-sectioning and negative staining) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The myocardial gap junctions are comprised of a single polypeptide of Mr 28,000, apparently derived from a protein of Mr 30,000. Hepatic gap junctions are also comprised of a single native protein of Mr 28,000 as previously reported. Exhaustive trypsin digestion of the isolated junctions cleaves both of these proteins similarly, while leaving their characteristic junctional lattice structures intact. However, comparison of heart and liver junctional proteins by two-dimensional peptide mapping of tryptic and α-chymotryptic fragments, followed by high pressure liquid chromatography, reveals no homology between these proteins.
AB - Gap junctions have been isolated from both rat heart and liver, tissues where junctions are typical in appearance and physiology. The purity of the fractions obtained was monitored by electron microscopy (thin-sectioning and negative staining) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The myocardial gap junctions are comprised of a single polypeptide of Mr 28,000, apparently derived from a protein of Mr 30,000. Hepatic gap junctions are also comprised of a single native protein of Mr 28,000 as previously reported. Exhaustive trypsin digestion of the isolated junctions cleaves both of these proteins similarly, while leaving their characteristic junctional lattice structures intact. However, comparison of heart and liver junctional proteins by two-dimensional peptide mapping of tryptic and α-chymotryptic fragments, followed by high pressure liquid chromatography, reveals no homology between these proteins.
UR - http://www.scopus.com/inward/record.url?scp=0021080021&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0021080021&partnerID=8YFLogxK
U2 - 10.1016/0092-8674(83)90188-5
DO - 10.1016/0092-8674(83)90188-5
M3 - Article
C2 - 6317197
AN - SCOPUS:0021080021
SN - 0092-8674
VL - 35
SP - 539
EP - 549
JO - Cell
JF - Cell
IS - 2 PART 1
ER -