Identification of albumin-synthesizing polysomes from mouse liver and a mouse hepatoma cell line

Peter C. Brown, John Papaconstantinou

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Albumin-synthesizing polysomes from mouse liver and mouse hepatoma cells in in tissue culture have been localized on sucrose gradients with 125I-labeled antimouse serum albumin used as a marker. Competition studies show that the 125I-labeled antibody binds specifically to albumin-synthesizing polysomes from both tissues. The 125I-labeled polysomes from liver and hepatoma cells have identical sedimentation properties on sucrose gradients, which indicates that the polysomes range in size from 9-14 ribosomes. This is comparable in size to polysomes from rat liver and Morris hepatoma. One significant difference between these albumin-synthesizing polysomes is that those extracted from hepatoma cells bind 70% less antibody than equivalent amounts of polysomes from liver cells. Since the level of albumin synthesis in the hepatoma cells is comparable to the level of albumin synthesis in vivo, this difference in antibody-binding capacity is not likely to be due to differences in polysomal content, but appears to be a characteristic difference between hepatoma and normal mouse liver cells.

Original languageEnglish (US)
Pages (from-to)121-128
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume76
Issue number1
DOIs
StatePublished - May 9 1977
Externally publishedYes

Fingerprint

Polyribosomes
Liver
Albumins
Hepatocellular Carcinoma
Cells
Cell Line
Sucrose
Antibodies
Tissue culture
Experimental Liver Neoplasms
Sedimentation
Serum Albumin
Rats
Ribosomes
Tissue

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Identification of albumin-synthesizing polysomes from mouse liver and a mouse hepatoma cell line. / Brown, Peter C.; Papaconstantinou, John.

In: Biochemical and Biophysical Research Communications, Vol. 76, No. 1, 09.05.1977, p. 121-128.

Research output: Contribution to journalArticle

@article{03919919e41e4d9bbee1fc9f6e662b10,
title = "Identification of albumin-synthesizing polysomes from mouse liver and a mouse hepatoma cell line",
abstract = "Albumin-synthesizing polysomes from mouse liver and mouse hepatoma cells in in tissue culture have been localized on sucrose gradients with 125I-labeled antimouse serum albumin used as a marker. Competition studies show that the 125I-labeled antibody binds specifically to albumin-synthesizing polysomes from both tissues. The 125I-labeled polysomes from liver and hepatoma cells have identical sedimentation properties on sucrose gradients, which indicates that the polysomes range in size from 9-14 ribosomes. This is comparable in size to polysomes from rat liver and Morris hepatoma. One significant difference between these albumin-synthesizing polysomes is that those extracted from hepatoma cells bind 70{\%} less antibody than equivalent amounts of polysomes from liver cells. Since the level of albumin synthesis in the hepatoma cells is comparable to the level of albumin synthesis in vivo, this difference in antibody-binding capacity is not likely to be due to differences in polysomal content, but appears to be a characteristic difference between hepatoma and normal mouse liver cells.",
author = "Brown, {Peter C.} and John Papaconstantinou",
year = "1977",
month = "5",
day = "9",
doi = "10.1016/0006-291X(77)91676-X",
language = "English (US)",
volume = "76",
pages = "121--128",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "1",

}

TY - JOUR

T1 - Identification of albumin-synthesizing polysomes from mouse liver and a mouse hepatoma cell line

AU - Brown, Peter C.

AU - Papaconstantinou, John

PY - 1977/5/9

Y1 - 1977/5/9

N2 - Albumin-synthesizing polysomes from mouse liver and mouse hepatoma cells in in tissue culture have been localized on sucrose gradients with 125I-labeled antimouse serum albumin used as a marker. Competition studies show that the 125I-labeled antibody binds specifically to albumin-synthesizing polysomes from both tissues. The 125I-labeled polysomes from liver and hepatoma cells have identical sedimentation properties on sucrose gradients, which indicates that the polysomes range in size from 9-14 ribosomes. This is comparable in size to polysomes from rat liver and Morris hepatoma. One significant difference between these albumin-synthesizing polysomes is that those extracted from hepatoma cells bind 70% less antibody than equivalent amounts of polysomes from liver cells. Since the level of albumin synthesis in the hepatoma cells is comparable to the level of albumin synthesis in vivo, this difference in antibody-binding capacity is not likely to be due to differences in polysomal content, but appears to be a characteristic difference between hepatoma and normal mouse liver cells.

AB - Albumin-synthesizing polysomes from mouse liver and mouse hepatoma cells in in tissue culture have been localized on sucrose gradients with 125I-labeled antimouse serum albumin used as a marker. Competition studies show that the 125I-labeled antibody binds specifically to albumin-synthesizing polysomes from both tissues. The 125I-labeled polysomes from liver and hepatoma cells have identical sedimentation properties on sucrose gradients, which indicates that the polysomes range in size from 9-14 ribosomes. This is comparable in size to polysomes from rat liver and Morris hepatoma. One significant difference between these albumin-synthesizing polysomes is that those extracted from hepatoma cells bind 70% less antibody than equivalent amounts of polysomes from liver cells. Since the level of albumin synthesis in the hepatoma cells is comparable to the level of albumin synthesis in vivo, this difference in antibody-binding capacity is not likely to be due to differences in polysomal content, but appears to be a characteristic difference between hepatoma and normal mouse liver cells.

UR - http://www.scopus.com/inward/record.url?scp=0017641519&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0017641519&partnerID=8YFLogxK

U2 - 10.1016/0006-291X(77)91676-X

DO - 10.1016/0006-291X(77)91676-X

M3 - Article

VL - 76

SP - 121

EP - 128

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -