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

Nutan T. Patel; Alexander Kurosky; Viktor Holoubek

doi:10.1016/0005-2795(78)90573-1

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 journal › Article › peer-review

4 Scopus citations

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 N^G-dimethylarginine (14% of total arginyl residues).

Original language	English (US)
Pages (from-to)	282-286
Number of pages	5
Journal	BBA - Protein Structure
Volume	533
Issue number	1
DOIs	https://doi.org/10.1016/0005-2795(78)90573-1
State	Published - Mar 28 1978
Externally published	Yes

ASJC Scopus subject areas

General Medicine

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10.1016/0005-2795(78)90573-1

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title = "Isolation and characterization of the predominant protein in nuclear ribonucleoprotein particles from rat liver",

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).",

author = "Patel, \{Nutan T.\} and Alexander Kurosky and Viktor Holoubek",

note = "Funding Information: herein. The presence of an unidentified basic amino acid residue was also reported to occur in informatin \textbackslash{}[15\textbackslash{}]. Informatin was previously believed to be the only protein of nuclear ribonucleoprotein particles (informofers) \textbackslash{}[1 5 \textbackslash{}] A full evaluation of the functional importance of the ribonucleoproteins must await further characterization of their role in nuclear RNA processing. A better understanding of the structure of these proteins will undoubtedly facilitate this evaluation. This work was supported by Grant H-393 from the Robert A. Welch Foundation. Copyright: Copyright 2014 Elsevier B.V., All rights reserved.",

year = "1978",

month = mar,

day = "28",

doi = "10.1016/0005-2795(78)90573-1",

language = "English (US)",

volume = "533",

pages = "282--286",

journal = "BBA - Protein Structure",

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publisher = "Elsevier BV",

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TY - JOUR

T1 - Isolation and characterization of the predominant protein in nuclear ribonucleoprotein particles from rat liver

AU - Patel, Nutan T.

AU - Kurosky, Alexander

AU - Holoubek, Viktor

N1 - Funding Information: herein. The presence of an unidentified basic amino acid residue was also reported to occur in informatin \[15\]. Informatin was previously believed to be the only protein of nuclear ribonucleoprotein particles (informofers) \[1 5 \] A full evaluation of the functional importance of the ribonucleoproteins must await further characterization of their role in nuclear RNA processing. A better understanding of the structure of these proteins will undoubtedly facilitate this evaluation. This work was supported by Grant H-393 from the Robert A. Welch Foundation. Copyright: Copyright 2014 Elsevier B.V., All rights reserved.

PY - 1978/3/28

Y1 - 1978/3/28

N2 - 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).

AB - 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).

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DO - 10.1016/0005-2795(78)90573-1

M3 - Article

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AN - SCOPUS:0017801412

SN - 0005-2795

VL - 533

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EP - 286

JO - BBA - Protein Structure

JF - BBA - Protein Structure

IS - 1

ER -

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

Abstract

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