Characterization of post-translationally modified ras p21 proteins and their in vitro and in vivo guanine nucleotide interactions
Ras p21 proteins were used for studying the biosynthesis and biochemistry of oncogene products. These proteins migrate as a heterogeneous series of polypeptides as resolved by both one- and two-dimensional polyacrylamide gel electrophoresis (PAGE). Polyspecific rat serum antibody to ras p21 was used to immunoprecipitate forms of p21 synthesized in vivo in transformed mammalian cell lines. Two-dimensional PAGE of p21 resolved two distinct groups of polypeptides, one acidic (pI 4.8-5.3) is denoted the A forms and one less acidic (pI 6.5-7.0) called the B forms. The membrane-localized B forms of v-ras-Ha p21 are predominantly phosphorylated in vivo. Pulse-chase experiments using ({sup 35}S)methionine show cytosolic precursor pro-p21 is the most acidic form processed within 4 hours to multiple membrane-localized polypeptides having higher isoelectric points. Modification(s) responsible for these multiple forms are unknown. Preliminary evidence suggests acylation inhibitor, cerulenin, partially blocks processing and/or membrane localization of pro-p21. The guanine nucleotide binding activities of p21 were also investigated.
- Research Organization:
- State Univ. of New York, Buffalo, NY (USA)
- OSTI ID:
- 5601052
- Resource Relation:
- Other Information: Thesis (Ph. D.)
- Country of Publication:
- United States
- Language:
- English
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IMMUNOASSAY
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SULFUR 35
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DAYS LIVING RADIOISOTOPES
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550201* - Biochemistry- Tracer Techniques