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Polynitroxylated pegylated hemoglobin (PNPH, VitalHeme™, SynZyme Technologies LLC, Irvine, CA) is a pegylated hemoglobin covalently labeled with catalytic nitroxides, aka caged nitric oxide (cNO). PNPH serves as a hyperoncotic biopolymer coated and redox transformed hemoglobin acting in the plasma phase as a neurovascular protective multifunctional nanomedicine. This drug is for the correction or prevention of inadequate regional and/or global blood flow without oxidative stress under normal or hypovolemic states in critical care and transfusion medicine. Specific clinical indications for which PNPH has shown efficacy are traumatic brain injury complicated by hemorrhagic shock, stroke, and sickle cell disease. PNPH may also be an ideal alternative to aged red blood cells and a bridge to transfusion.

Several new rifamycin derivatives have been synthesized and tested as inhibitors of an RNA-instructed DNA polymerase (RDP) function in an effort to determine the effect of rifamycin structure on RDP inhibition. It was found, in general, that RDP inhibition is favored by lipophilic tails bound to the 3 positions of rifamycin SV. Relative lipophilicities were measured by a reversed phase thin-layer chromatographic technique.

It is possible to design rifamycin derivatives which can distinguish between viral RNA-instructed DNA polymerase and other nucleotide polymerases.

The reaction catalyzed by nucleoside diphosphate kinase responds to the energy charge of the adenylate pool. The velocity is maximal at a charge of 1.0, and decreases sharply with a decrease in the charge. This response may control the flow of phosphate from ATP into the other nucleotide pools and thus participate in the regulation of macromolecular synthesis by the energy level of the cell, as reflected in the charge of the adenylate pool.

A reverse transcriptase activity, extracted from virus-transformed cells, is activated by very low concentrations of nonionic detergents. These same detergents also significantly reduce the effectiveness of certain rifamycin derivatives as inhibitors of the polymerase activity when the detergents are present at micelle-forming concentrations.