
The Binding of Extra Acidic Proteins to Deoxyribonucleoprotein during the Preparation of Nuclear Proteins
Author(s) -
Johns E. W.,
Forrester S.
Publication year - 1969
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1969.tb00561.x
Subject(s) - chemistry , cytoplasm , biochemistry , amino acid , nuclear protein , nuclear pore , transcription factor , gene
Acidic proteins can be removed from calf thymus deoxyribonucleoprotein, previously washed with 0.14 M NaCl, using 0.35 M NaCl. After the removal of these acidic proteins, the yield of acidic nuclear proteins as extracted by other methods dropped to less than one third. Calf thymus deoxyribonucleoprotein and reconstituted deoxyribonucleohistone adsorb acidic proteins from the cytoplasm and nuclear sap in 0.14 M NaCl. These proteins which can be released in 0.35 M NaCl are similar in amino acid analysis to the acidic nuclear proteins prepared by other methods.