Published April 1987
| Version v1
Report
Developmental regulation of tyrosine phosphorylation substrates calpactin 1 and vinculin in embryonic avian limb and expression in cultured limb cells
Description
Phosphotyrosine-containing proteins are minor components of normal cells that, in certain instances, are associated with the regulation of cellular metabolism and growth. An increase in the phosphotyrosine content of cellular proteins is observed following transformation by several avian sarcoma viruses. Two of the most prominent cellular substrates are calpactin 1 and vinculin. Both proteins are phosphorylated at tyrosine following transformation by retroviruses. To determine the sites of calpactin and vinculin synthesis frozen sections were prepared and stained with anti-calpactin and anti-vinculin serum
Additional details
Publishing Information
- Imprint Title
- Biology and Medicine Division: Annual report 1986
- Journal Page Range
- p. 251-254.
- Report number
- LBL--22300
INIS
- Country of Publication
- United States
- Country of Input or Organization
- United States
- INIS RN
- 19076525
- Subject category
- S60: APPLIED LIFE SCIENCES;
- Resource subtype / Literary indicator
- Progress Report
- Descriptors DEI
- AUTORADIOGRAPHY; CELL DIFFERENTIATION; FLUORESCENCE; HISTOLOGICAL TECHNIQUES; IMMUNOASSAY; MOLECULAR BIOLOGY; ONCOGENIC TRANSFORMATIONS; PROGRESS REPORT; PROTEINS; SULFUR 35; TYROSINE
- Descriptors DEC
- AMINO ACIDS; AROMATICS; BETA DECAY RADIOISOTOPES; BETA-MINUS DECAY RADIOISOTOPES; CARBOXYLIC ACIDS; DAYS LIVING RADIOISOTOPES; EMISSION; EVEN-ODD NUCLEI; HYDROXY ACIDS; ISOTOPES; LIGHT NUCLEI; LUMINESCENCE; NUCLEI; ORGANIC ACIDS; ORGANIC COMPOUNDS; PHOTON EMISSION; RADIOISOTOPES; SULFUR ISOTOPES