title: Cooperative ATP binding by cloned lamin C.
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 X 10(-6) and 2 X 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.
authors.affiliation: Department of Pathology, George Washington University, Washington, D.C. 20037.
authors.forename: A M
authors.initials: AM
authors.lastname: Schwartz
authors.forename: G A
authors.initials: GA
authors.lastname: Clawson
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D034904:Lamin Type A; D034882:Lamins; D009687:Nuclear Proteins / Q000378:metabolism*; D011485:Protein Binding; D011994:Recombinant Proteins / Q000378:metabolism
chemical_list: D034904:Lamin Type A; D034882:Lamins; D009687:Nuclear Proteins; D011994:Recombinant Proteins; C440308:lamin C; D000255:Adenosine Triphosphate