Molecular cloning and chromosomal localization of a novel Drosophila protein phosphatase

AbstractA 1.0 kilobase cDNA coding for the complete amino acid sequence of a putative protein phosphatase (314 amino acid residues, molecular mass 36 kDa) has been isolated from a Drosophila head cDNA library. The cDNA hybridises to a single site on the right arm of the second chromosome at cytological position 55A1–3. The deduced sequence of the protein, designated protein phosphatase-Y, is homologous to the catalytic subunits of Drosophila and rabbit protein phosphatase- 1α (64 and 59% identity, respectively) and rabbit protein phosphatase-2A (39% identity). These and other comparisons demonstrate that this novel enzyme is not the Drosophila counterpart of mammalian protein phosphatases 1, 2A, 2B, 2C or X

Cloning and regional localization of the mouse faciogenital dysplasia ( Fgd1 ) gene

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/47027/1/335_2004_Article_BF00352375.pd

Experimental evidence of parametric decay processes in the variable specific impulse magnetoplasma rocket (VASIMR) helicon plasma source

Decay waves have been observed in the megahertz range in the helium plasma generated by the variable specific impulse magnetoplasma rocket magnetoplasma thruster. They are measured using one of the tips of a triple probe connected to a 50 Ω input of a s