Sex ratios of the white-tailed antelope ground squirrel (Ammospermophilus leucurus), Indian Wells Valley, San Bernardino County, California

We studied the white-tailed antelope ground squirrel during spring and summer 2006 to determine young-of-the-year and adult sex ratios in the Indian Wells Valley, San Bernardino County, California. We calculated a young-of-the-year sex ratio of 1.45:1 (female to male), whereas the adult sex ratio was approximately 1:1. Our young-ofthe-year sex ratio was greater than the 1.1:1 (female to male) natal sex ratio previously reported. Differences between young-of-the-year and adult sex ratios may represent low female young-of-the-year survivorship in the Indian Wells Valley.     

DNA mutagenesis and recombination

The polymerase chain reaction is used for site-specific mutagenesis and for DNA recombination without any enzymatic reaction in vitro, apart from DNA amplification.     

The in vitro characterization of the inhibition of mouse brain protein kinase-C by retinoids and their receptors

Summary The mechanism of the in vitro inhibition of Ca²⁺-, phosphatidylserine-dependent protein kinase C (PK-C)² by the purifiedholo (ligand-saturated) forms of cellular retinol-binding protein (cRBP) and cellular retinoic acid-binding protein (cRABP) was studied. We report here that i) the PK-C-inhibitory action ofholo-cRBP andholo-cRABP is due to their respective ligands, all-trans-retinol and all-trans-retinoic acid; ii) the reduced phosphorylation of theholo-retinoid-binding proteins and brain cytosolic proteins is not the result of a retinoid-induced soluble phosphatase or protease activity; iii) retinoids reduce PK-C affinity for calcium and phosphatidylserine in vitro; and iv) the structure-function activity of the retinoids and the specific interaction of these effect of retinoids on plasma membrane-associated PK-C activity pays a significant role in defining the early epigenetic aspects of PK-C-dependent tumor promotion and may be a physiological mechanism by which retinoids induce terminal differentiation in cell types that do not express soluble retinoid-binding proteins.We would like to thank Dr L.M. De Luca (NIH, USA) for his contribution of retinylphosphate, Dr H.N. Bhagavan (Hoffmann-La Roche) for his contribution of the arotinoids, and Merrill-Dow Corp. for their contribution of difluoromethylornithine. This work was supported by NIH Grants CA-34968, CA-07175, CA-22484, and CA-09020.     

Hepatitis B polypeptide vaccine preparation in micelle form

The immunoprophylaxis of hepatitis B is hampered by the lack of a technique for growing hepatitis B virus (HBV) in tissue culture. Plasma from persistently infected individuals, one source of viral antigen, contains characteristic 22-nm spherical particles which share a common antigen (the hepatitis B surface antigen or HBsAg) with the outer envelope of the 42-nm double-shelled DNA virus. Highly purified inactivated 22-nm particles have been shown to be safe and to confer protective immunity against HBV in a recent large-scale clinical trial. We have already described the extraction from the particles of a complex of two proteins which are antigenic determinants of HBV--the polypeptide with molecular weight (MW) between 22,000 and 24,000 (called p23) and the glycosylated polypeptide (called gp28) with MW in the range 26,000--29,000 which is thought to be the glycosylated form of p23. We now report the preparation from this complex of water-soluble protein micelles which may be a suitable basis for a second-generation hepatitis B vaccine.