Cooperative ATP binding by cloned lamin C

Arnold M. Schwartz; Gary Clawson

doi:10.1016/0014-4827(91)90117-D

Cooperative ATP binding by cloned lamin C

Arnold M. Schwartz
, Gary Clawson

Research output: Contribution to journal › Article › peer-review

2 Scopus citations

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 language	English (US)
Pages (from-to)	432-434
Number of pages	3
Journal	Experimental Cell Research
Volume	193
Issue number	2
DOIs	https://doi.org/10.1016/0014-4827(91)90117-D
State	Published - Apr 1991

All Science Journal Classification (ASJC) codes

Cell Biology

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10.1016/0014-4827(91)90117-D

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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 × 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.",

author = "Schwartz, \{Arnold M.\} and Gary Clawson",

note = "Funding Information: This work was supported by NIH Grants CA21141, CA40145, and CA01003 and an award from the Elaine H. Snyder Trust.",

year = "1991",

month = apr,

doi = "10.1016/0014-4827(91)90117-D",

language = "English (US)",

volume = "193",

pages = "432--434",

journal = "Experimental Cell Research",

issn = "0014-4827",

publisher = "Elsevier Inc.",

number = "2",

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T1 - Cooperative ATP binding by cloned lamin C

AU - Schwartz, Arnold M.

AU - Clawson, Gary

N1 - Funding Information: This work was supported by NIH Grants CA21141, CA40145, and CA01003 and an award from the Elaine H. Snyder Trust.

PY - 1991/4

Y1 - 1991/4

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/0025763805

UR - https://www.scopus.com/pages/publications/0025763805#tab=citedBy

U2 - 10.1016/0014-4827(91)90117-D

DO - 10.1016/0014-4827(91)90117-D

M3 - Article

C2 - 2004657

AN - SCOPUS:0025763805

SN - 0014-4827

VL - 193

SP - 432

EP - 434

JO - Experimental Cell Research

JF - Experimental Cell Research

IS - 2

ER -

Cooperative ATP binding by cloned lamin C

Abstract

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