PubMed · 4514204
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R Grune. 1973. [Experiences with Kallocryl-A].. https://pubmed.ncbi.nlm.nih.gov/4514204/
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A novel method was used to examine the microbial ecology of iron-rich wetland sediments receiving neutral-pH coal mine drainage. Gel probes inserted into the sediments allowed analysis of the distribution and activity of bacterial sulfate reduction (BSR). A mixed population of sulfate-reducing bacteria enriched from anoxic wetland sediments was immobilized in low temperature-gelling agarose held in grooved rods or probes. The probes were inserted vertically into sediments and were allowed to incubate in situ for 48 h. After their retrieval, the gels were sectioned and analyzed for residual BSR activity and were compared to in situ BSR rates and chemical porewater profiles. The depth distribution of residual BSR activity in the immobilized cell gel probes differed significantly from the BSR measured in situ. Approximately 51% of the total integrated residual sulfate reduction activity measured in the gel probes occurred between 0 and 7 cm of the upper 20 cm of sediment. In contrast, ca. 99% of the integrated in situ BSR occurred between 7- and 20-cm depth, and only 1% of the total integrated rate occurred between 0- and 7-cm depth. Lactate-enriched bacteria immobilized in the gel may have been atypical of the majority of sulfate-reducing bacteria in the sediment. Agarose-immobilized sulfate-reducing bacteria might also be able to proliferate in the otherwise inhospitable zone of iron reduction, where sulfate and labile carbon compounds for which they are usually outcompeted can diffuse freely into the gel matrix. Gel probes containing particulate iron monosulfide (FeS) indicated that FeS remained stable in sediments at depths greater than 2 to 3 cm below the sediment-water interface, consistent with the shallow penetration of oxygen into surface sediments.
Poly-N-isopropylacrylamide (PNIPAAm) thermosensibility makes this polymer a very attractive candidate for controlled drug delivery systems. The polymer possesses a lower critical solution temperature (LCST) which was found to be around 32 degrees C in pure water, but which can be affected by the medium composition, i.e. presence of salts or surfactants. The knowledge of the effects of such substances on the LCST is very important while using PNIPAAm as a controlled drug delivery agent. The influence of a number of physiological and non-physiological salts and surfactants has been studied. The results obtained show that the addition of salts provokes an important decrease of the LCST of the polymer (salting out effect). A strong influence of the valence and of the size of the anions of the halide group was found. As to the surfactants, according to their type and concentration, a decrease or an increase of the LCST or even no effect at all were found. The effect of the GI secretions on the PNIPAAm phase separation temperature is also discussed.
This study was carried out to engineer N-isopropylacrylamide (NiPAM) polymers that contain protein-reactive N-acryloxysuccinimide (NASI) and hydrophobic alkylmethacrylates (AMAs). These thermoreversible, protein-conjugating polymers hold potential for retention of therapeutic proteins at an application site where tissue regeneration is desired. The lower critical solution temperatures (LCST) of the polymers were effectively controlled by the AMA mole content. The AMAs with longer side-chains were more effective in lowering the LCST. Polymers without NASI exhibited a stable LCST in phosphate buffer and in serum over a 10-day study period. The LCST of polymers containing NASI was found to increase over time in phosphate buffer, but not in serum-containing medium. The LCST increase in phosphate buffer was proportional to the AMA content. The feasibility of localizing a therapeutic protein, recombinant human bone morphogenetic protein-2 (rhBMP-2), to a site of application was explored in a rat intramuscular injection model. The results indicated that polymers capable of conjugating to rhBMP-2 were most effective in localizing the protein irrespective of the LCST (13-25 degrees C). For polymers with no NASI groups, a lower LCST resulted in a better rhBMP-2 localization. We conclude that thermosensitive polymers can be engineered for delivery of therapeutic proteins to improve their therapeutic efficacy.