Interactive cytogenetic effects on rat bone-marrow due to chronic ingestion of 2,5,2',5' and 3,4,3',4' PCBs.

Rats who were fed low doses of single PCBs, either 2,5,2',5' or 3,4,3',4', did not demonstrate any chromosome breakage or mitotic changes in their bone marrow cells. However, there was a significant increase in chromosome damage observed in bone marrow cells of rats ingesting 10 ppm 2,5,2',5' plus 0.1 ppm 3,3,3',4' in combination. It is suggested that this PCB combination, previously found to cause superadditive chromosome damage in vitro, is also capable of causing chromosome damage in vivo, but these effects do not compromise cell proliferation because the mitotic index is not depressed.     

Effect of salmon calcitonin on renal excretion of adenosine 3', 5' monophosphate in man.

Intravenous infusion of salmon calcitonin in six healthy subjects produced an increase in the plasma levels and urinary excretion of cyclic AMP. Cyclic AMP clearance diminished but remained higher than inulin clearance. Salmon calcitonin was also infused in six hypertensive patients with normal glomerular filtration rate. Arterial and renal venous plasma concentration of cyclic AMP were clearly raised. The difference between both these concentrations was not significant in the control periods but became marked during the treatment and post treatment periods demonstrating a net extraction of cyclic AMP from plasma by the kidneys. Renal extraction of cyclic AMP was lower than its urinary excretion in the control periods whereas it was clearly higher after salmon calcitonin was given. This shows that salmon calcitonin stimulates the production of cyclic AMP in extra-renal tissues and that the excess of cyclic AMP formed is catabolized by the kidneys.     

Integrons found in different locations have identical 5' ends but variable 3' ends.

The positions of the outer boundaries of the 5'- and 3'-conserved segment sequences of integrons found at several different locations have been determined. The position of the 5' end of the 5'-conserved segment is the same for six independently located integrons, In1 (R46), In2 (Tn21), In3 (R388), In4 (Tn1696), In5 (pSCH884), and In0 (pVS1). However, the extent of the 3'-conserved segment differs in each integron. The sequences of In2 and In0 diverge first from the conserved sequence, and their divergence point corresponds to the 3'-conserved segment endpoint defined previously (H.W. Stokes and R.M. Hall, Mol. Microbiol. 3:1669-1683, 1989), which now represents the endpoint of a 359-base deletion in In0 and In2. The sequence identity in In3, In1, In4, and In5 extends beyond this point, but each sequence diverges from the conserved sequence at a different point within a short region. Insertions of IS6100 were identified adjacent to the end of the conserved region in In1 and 123 bases beyond the divergence point of In4. These 123 bases are identical to the sequence found at the mer end of the 11.2-kb insertion in Tn21 but are inverted. In5 and In0 are bounded by the same 25-base inverted repeat that bounds the 11.2-kb insert in Tn21, and this insert now corresponds to In2. However, while In0, In2, and In5 have features characteristic of transposable elements, differences in the structures of these three integrons and the absence of evidence of mobility currently preclude the identification of all of the sequences associated with a functional transposon of this type.     

Culic 3', 5', -adenosine monophosphate and catabolic repression in Escherichia coli.

Several strains of $\text{E. coli}$ were grown on different sources of carbon and β-galactosidase activity as well as intracellular and extracellular concentrations of c-AMP were determined. There was a good (inverse) correlation between extracellular concentrations of c-AMP and the intensity of catabolite repression, whereas the relationship between intracellular c-AMP levels and catabolite repression was not clear-cut.     

Radioimmunoassay of cytidine 3',5' monophosphate (cCMP). I. Development of the assay.

A method is presented for the production of reagents for a radioimmunoassay for cCMP. cCMP was succinylated at the 2′0 position with [1,4 ¹⁴C] succinic anhydride, and the monosuccinyl cCMP coupled to Keyhole limpet hemocyanin and injected into rabbits. Antibodies to cCMP were produced that showed minimal crossreactivity with other cyclic nucleotides. Monosuccinyl cCMP was coupled to tyrosine methyl ester, then labeled with ¹²⁵I, and used as the radiolabeled ligand in the immunoassay of cCMP. By use of this assay, the concentration of cCMP in various tissues of rat and guinea pig have been determined.