Two-Dimensional Gel Electrophoresis of Acid-extractable Nuclear Proteins of Regenerating and Thioacetamide-treated Rat Liver, Morris 9618A Hepatoma, and Walker 256 Carcinosarcoma1

نویسندگان

  • Lynn C. Yeoman
  • Charles W. Taylor
  • Harris Busch
چکیده

The acid-soluble nuclear proteins of regenerating and thioacetamide-treated rat livers as well as the Morris 9618A hepatoma and the Walker 256 carcinosarcoma were ex tracted from citric acid-isolated nuclei with 0.4 N H2SO4. The nuclear extracts were analyzed by two-dimensional polyacrylamide gel electrophoresis. Although most of the protein spots were common to the livers and tumors stud ied, all of the rodent tumors were similar in their marked density of Spots C16-C18. In normal, regenerating, and thioacetamide-treated liver, the spots in this region were much less dense.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Two-dimensional gel electrophoresis of acid-extractable nuclear proteins of regenerating and thioacetamide-treated rat liver, Morris 9618a hepatoma, and Walker 256 carcinosarcoma.

The acid-soluble nuclear proteins of regenerating and thioacetamide-treated rat livers as well as the Morris 9618A hepatoma and the Walker 256 carcinosarcoma were ex tracted from citric acid-isolated nuclei with 0.4 N H2SO4. The nuclear extracts were analyzed by two-dimensional polyacrylamide gel electrophoresis. Although most of the protein spots were common to the livers and tumors stud ied, ...

متن کامل

Two-dimensional gel electrophoresis of acid-soluble nucleolar proteins of Walker 256 carcinosarcoma, regenerating liver, and thioacetamide-treated liver.

The acid-extractable proteins of nucleoli of Walker 256 carcinosarcoma, regenerating rat liver, and thioacetamidetreated rat liver were separated into 91, 94, and 92 spots, respectively, by two-dimensional polyacrylamide gel electrophoresis. Although the protein patterns from these different nucleoli have remarkable similarities, some qualitative and quantitative differences were found among th...

متن کامل

Lectin-binding Proteins in Nuclear Preparations from Rat Liver and Malignant Tumors1

l cd in binding (concanavalin A, biotinv lated ricinus communis agglutinin, and biotinylated siiccinylated wheat germ agglutinin (B-SWGA)) was used to detect the glycosylated proteins associated with a residual protein fraction [insoluble in 4% sodium dodecyl sulfate and termed the nuclear residual fraction (NRF)] or with nuclear matrix preparations from normal rat liver, azo dye (3'-MeDAB)-ind...

متن کامل

Lectin-binding proteins in nuclear preparations from rat liver and malignant tumors.

Lectin binding [concanavalin A, biotinylated ricinus communis agglutinin, and biotinylated succinylated wheat germ agglutinin (B-SWGA)] was used to detect the glycosylated proteins associated with a residual protein fraction [insoluble in 4% sodium dodecyl sulfate and termed the nuclear residual fraction (NRF)] or with nuclear matrix preparations from normal rat liver, azo dye (3'-MeDAB)-induce...

متن کامل

A comparison of polysomal messenger ribonucleoprotein particles from normal and neoplastic rat liver.

Free polysomes were isolated from normal and regenerating rat liver and from Morris hepatomas 7777, 7800, 5123C and 9618A. Sucrose gradient analysis ruled out the possibility of any significant messenger RNA degradation in these polysome preparations. The ethylenediaminetetraacetate-disrupted polysomes were fractionated on oligodeoxythymidylic acid-cellulose columns. The column-bound polyriboad...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2006