Literature DB >> 4346753

Isolation of arginine acceptor-proteins from normal rat liver and Novikoff hepatoma supernatant.

J Pinard, G de Lamirande.   

Abstract

In the present report a procedure for the isolation of more specific arginine receptors from the soluble fraction of rat liver and Novikoff hepatoma is described. In normal rat liver the specific activity of these receptors from the soluble fraction of rat liver and Novikoff hepatoma is described. In normal rat liver the specific activity of these receptors is fifteen times greater than that of the other proteins whereas in the Novikoff it is only three to four times higher. Attempts to sub-fractionate this class of acceptors would seem to indicate a relative homogeneity.

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Year:  1973        PMID: 4346753      PMCID: PMC2008823          DOI: 10.1038/bjc.1973.3

Source DB:  PubMed          Journal:  Br J Cancer        ISSN: 0007-0920            Impact factor:   7.640


  13 in total

1.  The distribution and chemical composition of ultracentrifugally separated lipoproteins in human serum.

Authors:  R J HAVEL; H A EDER; J H BRAGDON
Journal:  J Clin Invest       Date:  1955-09       Impact factor: 14.808

2.  Protein measurement with the Folin phenol reagent.

Authors:  O H LOWRY; N J ROSEBROUGH; A L FARR; R J RANDALL
Journal:  J Biol Chem       Date:  1951-11       Impact factor: 5.157

3.  Arginine incorporation into proteins by supernatant fractions of rat liver and Novikoff hepatoma.

Authors:  M Dupras; G De Lamirande
Journal:  Cancer Res       Date:  1970-05       Impact factor: 12.701

4.  Incorporation of [14C]arginine into rat liver proteins catalysed by soluble enzymes only.

Authors:  D M Gill
Journal:  Biochim Biophys Acta       Date:  1967

5.  A soluble enzyme from Escherichia coli which catalyzes the transfer of leucine and phenylalanine from tRNA to acceptor proteins.

Authors:  M J Leibowitz; R L Soffer
Journal:  Biochem Biophys Res Commun       Date:  1969-07-07       Impact factor: 3.575

6.  Enzymatic modification of proteins. II. Purification and properties of the arginyl transfer ribonucleic acid-protein transferase from rabbit liver cytoplasm.

Authors:  R L Soffer
Journal:  J Biol Chem       Date:  1970-02-25       Impact factor: 5.157

7.  The fractionation of high-molecular-weight ribonucleic acid by polyacrylamide-gel electrophoresis.

Authors:  U E Loening
Journal:  Biochem J       Date:  1967-01       Impact factor: 3.857

8.  Further studies on the soluble amino acid incorporating system from rat liver.

Authors:  H Kaji
Journal:  Biochemistry       Date:  1968-11       Impact factor: 3.162

9.  Enzymic modification of proteins. I. General characteristics of the arginine-transfer reaction in rabbit liver cytoplasm.

Authors:  R L Soffer; H Horinishi
Journal:  J Mol Biol       Date:  1969-07-14       Impact factor: 5.469

10.  Ribonuclease-resistant incorporation of phenylalanine into protein by a soluble system from trout liver.

Authors:  L Rosen; G D Novelli
Journal:  Biochim Biophys Acta       Date:  1967-08-22
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