Differential effect of pH on solubilization of nuclear lamins A/C and lamin B.
Extraction of isolated rat liver nuclear envelopes with 4M urea at various pH values led to differential solubilization of lamin polypeptides. All three lamins A, B and C were solubilized to 70-80% when extraction was performed at pH 8 while only 50-60% of lamins A and C were solubilized at pH 6, leaving lamin B completely insoluble. These results indicated that the interaction of lamin B with the nuclear envelope was strongly dependent upon the ionization state of lamin B and/or of its putative attachment site.
Raymond
Y
Y
Institut du Cancer de Montréal, Québec, Canada.
D000818:Animals; D001665:Binding Sites; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D034921:Lamin Type B; D034882:Lamins; D008099:Liver / Q000032:analysis; D008297:Male; D009685:Nuclear Envelope / Q000378:metabolism; D009687:Nuclear Proteins / Q000302:isolation & purification* / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D012995:Solubility
D034921:Lamin Type B; D034882:Lamins; D009687:Nuclear Proteins