Purification and characterization of a 43,000 dalton "DNAase binding protein" distinct from actin.

Abstract:

:"DNase binding protein" of 43K daltons as determined by SDS-polyacrylamide gel electrophoresis, was purified from the 0.1 M KCl-soluble (non-structural) fraction of chicken skeletal muscle. The protein was distinct from actin in amino acid composition and physicochemical properties. "DNase binding protein" was also isolated from other kinds of muscle and non-muscle cells. The ratio of the amino acid incorporation rate of "DNAase binding protein" to that of actin is different skeletal and smooth muscle and non-muscle cells.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Kohama K,Holtzer H

doi

10.1093/oxfordjournals.jbchem.a133208

subject

Has Abstract

pub_date

1981-02-01 00:00:00

pages

341-9

issue

2

eissn

0021-924X

issn

1756-2651

journal_volume

89

pub_type

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