Characterization of rat liver cells transformed in culture bydl-ethionine

In Vitro ◽  
1984 ◽  
Vol 20 (4) ◽  
pp. 291-301 ◽  
Author(s):  
Ursula I. Heine ◽  
Mary J. Wilson ◽  
Eliana F. Munoz
Keyword(s):  
Rat Liver ◽  
Liver Cells ◽  
Rat Liver Cells

Characterization of Isolated Rat-Liver Cells Made Permeable with Filipin

1981 ◽  
Vol 119 (2) ◽  
pp. 409-414 ◽  
Author(s):  
Henk S. GANKEMA ◽  
Elly LAANEN ◽  
Albert K. GROEN ◽  
Joseph M. TAGER
Keyword(s):  
Rat Liver ◽  
Liver Cells ◽  
Isolated Rat Liver ◽  
Rat Liver Cells ◽  
Isolated Rat

scholarly journals Structure and metabolism of rat liver heparan sulphate

1977 ◽  
Vol 164 (1) ◽  
pp. 75-81 ◽  
Author(s):  
Åke Oldberg ◽  
Magnus Höök ◽  
Björn Öbrink ◽  
Håkan Pertoft ◽  
Kristofer Rubin
Keyword(s):  
Rat Liver ◽  
Membrane Fraction ◽  
Glucuronic Acid ◽  
Heparan Sulphate ◽  
Primary Cultures ◽  
Liver Cells ◽  
Guanidinium Chloride ◽  
Rat Liver Cells ◽  
Structure And Metabolism

Rat liver cells grown in primary cultures in the presence of [35S]sulphate synthesize a labelled heparan sulphate-like glycosaminoglycan. The characterization of the polysaccharide as heparan sulphate is based on its resistance to digestion with chondroitinase ABC or hyaluronidase and its susceptibility to HNO2 treatment. The sulphate groups (including sulphamino and ester sulphate groups) are distributed along the polymer in the characteristic block fashion. In 3H-labelled heparan sulphate, isolated after incubation of the cells with [3H]galactose, 40% of the radioactive uronic acid units are l-iduronic acid, the remainder being d-glucuronic acid. The location of heparan sulphate at the rat liver cell surface is demonstrated; part of the labelled polysaccharide can be removed from the cells by mild treatment with trypsin or heparitinase. Further, a purified plasma-membrane fraction isolated from rats previously injected with [35S]sulphate contains radioactively labelled heparan sulphate. A proteoglycan macromolecule composed of heparan sulphate chains attached to a protein core can be solubilized from the membrane fraction by extraction with 6m-guanidinium chloride. The proteoglycan structure is degraded by treatment with papain, Pronase or alkali. The production of heparan [35S]sulphate by rat liver cells incubated in the presence of [35S]sulphate was followed. Initially the amount of labelled polysaccharide increased with increasing incubation time. However, after 10h of incubation a steady state was reached where biosynthetic and degradative processes were in balance.

scholarly journals Cloning and functional characterization of the bile acid-sensitive methotrexate carrier from rat liver cells

Hepatology ◽  
2000 ◽  
Vol 31 (6) ◽  
pp. 1296-1304 ◽  
Author(s):  
Walther Honscha ◽  
Kerstin U. Dötsch ◽  
Nadine Thomsen ◽  
Ernst Petzinger
Keyword(s):  
Bile Acid ◽  
Rat Liver ◽  
Functional Characterization ◽  
Liver Cells ◽  
Rat Liver Cells

scholarly journals Purification and characterization of the protein kinase eEF-2 isolated from rat liver cells.

1994 ◽  
Vol 41 (4) ◽  
pp. 421-427
Author(s):  
A Gajko ◽  
W Gałasiński ◽  
A Gindzieński
Keyword(s):  
Protein Kinase ◽  
Rat Liver ◽  
Elongation Factor ◽  
Liver Cells ◽  
Relative Molecular Mass ◽  
Purification And Characterization ◽  
Elongation Factor 2 ◽  
Inactive Form ◽  
Rat Liver Cells

The elongation factor 2 (eEF-2) protein kinase was isolated from rat liver cells, purified and partly characterized. It was found that the enzyme exists in an inactive form in the homogenate of rat liver. The active fraction of kinase eEF-2 was obtained after removal of the inhibitory substance by hydroxyapatite column chromatography. The purified enzyme is an electrophoretically homogeneous protein with relative molecular mass of approximately 90,000 and isoelectric point, pI = 5.9. The enzyme specifically phosphorylates the elongation factor eEF-2 in the presence of calmodulin and Ca2+.

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