TY - JOUR
T1 - The major nucleoside triphosphatase of nuclear scaffold is distinct from actin
AU - Clawson, Gary A.
AU - Lackey, Angela
AU - Button, Jane
AU - Smuckler, Edward A.
N1 - Funding Information:
We thank David Geller for fine editorial assistance. This work was supported in part by USPHS Grants CA21141, CA40145. a Research Career Development Award (K04 CA01003); a UCSF Academic Senate Award, and a grant from the Council for Tobacco Research.
PY - 1986/12
Y1 - 1986/12
N2 - 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.
AB - 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.
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U2 - 10.1016/0014-4827(86)90195-3
DO - 10.1016/0014-4827(86)90195-3
M3 - Article
C2 - 3021484
AN - SCOPUS:0022966652
SN - 0014-4827
VL - 167
SP - 559
EP - 562
JO - Experimental Cell Research
JF - Experimental Cell Research
IS - 2
ER -