Abstract

Cloned human lamin C was expressed in and purified from bacteria and used in ATP binding assays. Scatchard analysis revealed strong positive cooperative and noncooperative binding, with estimated apparent dissociation constants of 3 × 10-6 and 2 × 10-5 M, respectively. The binding is strongly pH dependent. ATP binding by lamins A C (presumably as intermediate filaments) may provide a substantial storage depot for ATP at the peripheral lamina for use by a number of ATP-requiring nuclear scaffold enzymes.

Original languageEnglish (US)
Pages (from-to)432-434
Number of pages3
JournalExperimental Cell Research
Volume193
Issue number2
DOIs
StatePublished - Jan 1 1991

Fingerprint

Adenosine Triphosphate
Lamin Type A
Nuclear Matrix
Intermediate Filaments
Bacteria
lamin C
Enzymes

All Science Journal Classification (ASJC) codes

  • Cell Biology

Cite this

Schwartz, Arnold M. ; Clawson, Gary. / Cooperative ATP binding by cloned lamin C. In: Experimental Cell Research. 1991 ; Vol. 193, No. 2. pp. 432-434.
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Cooperative ATP binding by cloned lamin C. / Schwartz, Arnold M.; Clawson, Gary.

In: Experimental Cell Research, Vol. 193, No. 2, 01.01.1991, p. 432-434.

Research output: Contribution to journalArticle

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