The more insoluble polypeptides of the avian erythrocyte nuclear envelope have been characterized by a two-dimensional electrophoretic procedure. Most of the polypeptides occur in two classes with isoelectric points of approximately 6.4 and 5.7 respectively. The more acidic class contains two polypeptides, P71 and one which contributes to an electrophoretic band previously identified as P55. The more basic class includes P75, P68, P61 and two or more polypeptides from the P55 band. There are four to six isoelectric point variants of each polypeptide in the more basic class, and the relative stain intensities for the variants are similar for the different polypeptides. These similarities in ionic properties suggest a chemical relationship between the polypeptides. These results are discussed in relation to the in vitro conversion of P75 to polypeptides of the same molecular weight as P68, P61 and P55. © 1979.
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