A lambda L 47.1 clone library was constructed from BamHI digests of cellular cat DNA and was screened with cDNA probes specific for the 3'-terminus of the replication competent RD-114 virus. The first analysis of one clone (lambda-ECE 1) shows that it consists at least of a 3'-LTR and a 5' adjacent env gene. The LTR nucleotide sequences of the RD-114 cDNA clones and ECE 1 are identical within the R region and unrelated to FeLV. Otherwise, the region upstream from the 3'-LTR of ECE 1 shows homology to the transmembrane protein encoding gene of FeLV, but not to RD-114. These results imply that ECE 1 is a recombinant between an RD-114-like 3'-LTR and a FeLV-related env portion.

An atmospheric emission line centered at 22,235 MHz has been detected repeatedly over the period of March-August 1975 with a radio telescope located at Westford, Massachusetts (42.5øN, 71.5øW). The line has also been detected in absorption against the sun's microwave continuum. From its exact coincidence in frequency with the well-known 1.3-cm line of the water molecule the line is identified with atmospheric water vapor. A mixing ratio distribution between altitudes of 50 and 80 km is derived from the measured line amplitude and shape. Mixing ratios as large as 15 ppm by volume, about 2 times larger than the maximum predicted by photochemical equilibrium calculations, are found at these mesospheric altitudes.

9S globin mRNA prepared by the proteinase K method from polysomes of rabbit reticulocytes consists of 40% circular molecules as revealed by electron microscopy, if spreading of the molecules is performed from a solution of 50% formamide, 0.5 M NaCl, 25 mM Tris, 10 mM EDTA, pH 8, after 16 h incubation at 42 degrees C. We assume a noncovalent nature of the circularization because of the fact that a total transformation into the well known linear form occurs if strong denaturing conditions for spreading were used. The biological significance of the circular globin mRNA molecules is unknown.

The amino acid sequence of insulin of carp (Cyprinus carpio) has been determined and correlated with its biological activity in a fat-cell test and its structural properties as measured by circular dichroism and sedimentation analysis.The amino acid sequence of carp insulin displays some unusual features: the B chain is longer at the N terminus by two residues as compared with mammalian insulins and there are substitutions of the charged residues, found in most insulins at positions B21 and B22, by proline and threonine respectively. On the other hand, all amino acid residues essential for biological activity and for the association of insulin monomers are the same in carp insulin. Accordingly, the half-maximal response in a fat-cell test is reached with carp insulin at concentrations which are only three times higher than with porcine insulin and the maximal response is the same. The circular dichroism spectrum of carp insulin resembles greatly that of bovine insulin indicating that it has a similar spatial structure. Despite amino acid substitutions in the dimer-dimer contact region, carp insulin is able to form hexamers.

The nucloic acid sequence of the preproinsulin cDNA of carp Calculatione based on the comparison of known preproinsulin cONA sequences showed that the evolutionary distance between fresh water and salt water toloostians is not smaller than between man and chicken.