Fig. 2.
![Fig. 2. In vitro kinase activity of wild-type TEL/PDGFβR fusion protein in Ba/F3 cells. / (A) Cells were lysed and immunoprecipitated with antibody recognizing the PDGFβR cytoplasmic domain. Immunoprecipitates were washed, subjected to in vitro phosphorylation with γ-[32P]-ATP, and separated by SDS-PAGE. (B) Radiolabeled wild-type TEL/PDGFβR was excised from the gel, acid hydrolyzed to constituent phosphoamino acids, and separated by 2-dimensional electrophoresis. (C) Immune complex kinase assay was performed as above using lysates from 32D cells that express TEL/PDGFβR variants. Phosphorylation of exogenous purified GST-p97 (GST-Gab2) was determined. Expression of TEL/PDGFβR and variants was equivalent in each of the cell lines (data not shown).](https://ash.silverchair-cdn.com/ash/content_public/journal/blood/98/12/10.1182_blood.v98.12.3390/6/h82311781002.jpeg?Expires=1735825329&Signature=lS5DuYIhfzSUryW0q6x4M0Y24TpMZ8d2zX-BKGsqS~e5fdJCoSBwDkqY6UKRNfPAQ9Dx-GzR7h3ck8JJP6lPtS~vIObZ05DgI2gP8U0a3-Ta49cc6KNUcr1guUv75dK8x6jp76lk8x3eUGW2OBCdELQylHvYyhWXoziX7-iJNfMmQ5oocJBeCP0dclffaDiZcrdFNo5npdGVElrXcjrJ69ojjMl2KUNIJnzVJgO-wuJl4TNALo-4AnKGoqKaacJ0LQz0iQz2v6Ym-qzHHeUddtZoRN0dbZh2ztwWqE1W8PUD8QtJ4tcNPw9QcDXrvW6xQ1XZY0VYNse8rkB~RHhRsw__&Key-Pair-Id=APKAIE5G5CRDK6RD3PGA)
In vitro kinase activity of wild-type TEL/PDGFβR fusion protein in Ba/F3 cells.
(A) Cells were lysed and immunoprecipitated with antibody recognizing the PDGFβR cytoplasmic domain. Immunoprecipitates were washed, subjected to in vitro phosphorylation with γ-[32P]-ATP, and separated by SDS-PAGE. (B) Radiolabeled wild-type TEL/PDGFβR was excised from the gel, acid hydrolyzed to constituent phosphoamino acids, and separated by 2-dimensional electrophoresis. (C) Immune complex kinase assay was performed as above using lysates from 32D cells that express TEL/PDGFβR variants. Phosphorylation of exogenous purified GST-p97 (GST-Gab2) was determined. Expression of TEL/PDGFβR and variants was equivalent in each of the cell lines (data not shown).
