The major nucleoside triphosphatase of nuclear scaffold is distinct from actin

Gary Clawson, Angela Lackey, Jane Button, Edward A. Smuckler

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

The major nucleoside triphosphatase of rat liver nuclear scaffold, a 46 kD protein thought to participate in nucleocytoplasmic RNA translocation, is distinct from immunologically-identified scaffold actin on Western blots, has a substantially different amino acid composition, and its enzymatic activity is not affected by anti-actin antibodies. Thus, although the contractile protein actin is found in nuclear scaffold and appears to interact with RNA, it is not associated with the nucleoside triphosphatase activity in such preparations.

Original languageEnglish (US)
Pages (from-to)559-562
Number of pages4
JournalExperimental Cell Research
Volume167
Issue number2
DOIs
StatePublished - Jan 1 1986

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Nucleoside-Triphosphatase
Nuclear Matrix
Actins
RNA
Contractile Proteins
Anti-Idiotypic Antibodies
Western Blotting
Amino Acids
Liver
Proteins

All Science Journal Classification (ASJC) codes

  • Cell Biology

Cite this

Clawson, Gary ; Lackey, Angela ; Button, Jane ; Smuckler, Edward A. / The major nucleoside triphosphatase of nuclear scaffold is distinct from actin. In: Experimental Cell Research. 1986 ; Vol. 167, No. 2. pp. 559-562.
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The major nucleoside triphosphatase of nuclear scaffold is distinct from actin. / Clawson, Gary; Lackey, Angela; Button, Jane; Smuckler, Edward A.

In: Experimental Cell Research, Vol. 167, No. 2, 01.01.1986, p. 559-562.

Research output: Contribution to journalArticle

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