A cAMP binding protein was detected in HL-60 cells using photoaffinity labeling with 8-azido ["PIcAMP. The binding protein was found i n a 0.35 M NaCl nuclear protein extract from untreated HL-60 cells and from the HL-60 cells induced to mature with retinoic acid. While the quantity of the cAMP bind
Retinoic acid inhibits the myristoylation of a membrane protein in HL-60 cells
β Scribed by M. Almagor; J. Bar-Tana
- Book ID
- 115762923
- Publisher
- Elsevier Science
- Year
- 1990
- Tongue
- English
- Weight
- 337 KB
- Volume
- 172
- Category
- Article
- ISSN
- 0006-291X
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π SIMILAR VOLUMES
HL-60 cells were incubated with ["Pl-P, in order to label endogenous phosphoproteins in situ. These were then resolved via two-dimensional electrophoresis and autoradiograms were made from the gels. A comparison of autoradiograms made from rctinoic-acid-differentiated cells with those made from cont
We previously observed that HL-60 cells treated with manganese (Mn) during differentiation displayed an enhanced oxidative burst. Since a Mn-dependent kinase has been identified and phosphorylation is involved in burst activation, the objective of this research was to identify proteins in retinoic a