Background: B-Type natriuretic peptide (BNP 1-32 ) as well as the N-terminal fragment of the prohormone containing residues 1-76 (NT-proBNP 1-76 ), both cleavage products of the precursor proBNP 1-108 , are reported to be powerful markers for prognosis and risk stratification of heart failure. However, the intact precursor also circulates in the bloodstream. Assays for the detection of these cleavage products have been developed, but most of these assays may overestimate the concentrations of the cleavage products because they also measure the precursor form. It is therefore important to develop an immunoassay that specifically measures solely proBNP 1-108 in plasma. Methods: After carefully designing the peptide used to immunize mice, we selected a specific monoclonal antibody (mAb Hinge76) that recognizes the cleavage site of proBNP 1-108 , an epitope present only in the precursor form. mAb Hinge76 recognizes recombinant proBNP 1-108 in a dose-dependent manner, without any significant cross-reactivity with either recombinant NT-proBNP 1-76 or synthetic BNP 1-32 . By combining mAb Hinge76 with a polyclonal antibody directed against BNP 1-32 , we were able to set up a proBNP 1-108 -specific sandwich immunoassay able to confirm the presence of proBNP 1-108 in blood samples. Results: From a cohort of 50 healthy persons and 170 patients with congestive heart failure (CHF), our assay was able to differentiate healthy individuals from CHF patients (P <0.005). Interestingly, plasma proBNP 1-108

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Synthesis of the proteins of rabies virus was studied in hamster cells infected with UV-irradiated virus. The UV target size of genes L, N, Ml, and M2 was measured during primary transcription. Except for N, the target size of the remaining genes was considerably larger than that of their physical sizes. The data fit the hypothesis that four genes occupy a single transcriptional unit and that transcription of rabies virus proceeds in the order N, Ml, M2, and L.

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SUMMARYAn RNA polymerase activity has been demonstrated in purified rabies virions. Efficiency of the reaction is low since the rate of incorporation was equal to 3 to 5 pmol of uridine per hour, per mg of protein. As with other mammalian rhabdoviruses the optimal temperature was 31 °C. Unlike vesicular stomatitis virus, manganese could be substituted for magnesium as a divalent cation, at an optimum concentration of Io to 20 mM.