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Comparison of the major polypeptides of the erythrocyte nuclear envelope

✍ Scribed by Cochran, David L. ;Egle, Patsy M. ;Shelton, Keith R. ;Yeoman, Lynn C.

Publisher
Wiley (John Wiley & Sons)
Year
1979
Tongue
English
Weight
944 KB
Volume
10
Category
Article
ISSN
0091-7419

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✦ Synopsis

The three most abundant nonhistone polypeptides (molecular weights 75,000, 7 1,000 and 61,000) of the avian erythrocyte nucleus have previously been iso- lated in the nuclear envelope fraction. They have been separated by sodium dodecylsulfate-polyacrylamide gel electrophoresis and peptide-mapped after limited enzymatic digestion. Three enzymes -chymotrypsin, papain and Staphylococcus aureus protease -were used. Results obtained with each enzyme indicate strong similarities between the three nuclear envelope polypeptides. The amino acid compositions of the two most abundant polypeptides (P75 and P7 1) have been determined and found to be similar. Further, they readily yield large fragments upon brief alkaline hydrolysis. For both P75 and P71 the degree and the pattern of alkaline fragmentation are almost identical. A 61.000-dalton polypeptide which appears t o be P61 is obtained from P75 and P7 1 by mild acid hydrolysis. These results establish the close chemical similarity of these predominant polypeptides in the erythrocyte nucleus and suggest that they serve related functions.

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