Isolation and characterization of the predominant protein in nuclear ribonucleoprotein particles from rat liver

Nutan T. Patel, Alexander Kurosky, Viktor Holoubek

    Research output: Contribution to journalArticle

    4 Citations (Scopus)

    Abstract

    The predominant protein of the nuclear ribonucleoprotein particles of rat liver was isolated by polyacrylamide gel electrophoresis. The polypeptide represented 35% to 40% of the total mass of the protein moiety. Its molecular weight was estimated to be 38 000 and its NH2-terminal residue was found to be threonine. The amino acid composition is unique in having a high content of glycyl residues (20%) and NG-dimethylarginine (14% of total arginyl residues).

    Original languageEnglish (US)
    Pages (from-to)282-286
    Number of pages5
    JournalBBA - Protein Structure
    Volume533
    Issue number1
    DOIs
    StatePublished - Mar 28 1978

    Fingerprint

    Ribonucleoproteins
    Threonine
    Nuclear Proteins
    Electrophoresis
    Liver
    Rats
    Polyacrylamide Gel Electrophoresis
    Molecular Weight
    Molecular weight
    Amino Acids
    Peptides
    Chemical analysis
    Proteins
    polyacrylamide gels
    dimethylarginine

    ASJC Scopus subject areas

    • Medicine(all)

    Cite this

    Isolation and characterization of the predominant protein in nuclear ribonucleoprotein particles from rat liver. / Patel, Nutan T.; Kurosky, Alexander; Holoubek, Viktor.

    In: BBA - Protein Structure, Vol. 533, No. 1, 28.03.1978, p. 282-286.

    Research output: Contribution to journalArticle

    Patel, Nutan T. ; Kurosky, Alexander ; Holoubek, Viktor. / Isolation and characterization of the predominant protein in nuclear ribonucleoprotein particles from rat liver. In: BBA - Protein Structure. 1978 ; Vol. 533, No. 1. pp. 282-286.
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