Modified lipids chemical methods

Central to addressing those biological problems described earlier is the ability to produce posttranslationally modified (lipidated) proteins and to introduce reporter groups into these proteins as a read-out for protein activity. These issues are largely solved by using chemical methods as described in later sections. 

To correlate embryonic arrests with the metabolic pathways, and especially to understand why cellular organelles first undergo chemical damages, biological investigations include evaluation of DNA, RNA, protein, glucose, lipid, and adenosine-5 -triphosphate (ATP) contents, whose fractions are extracted and isolated by modified Schneider methods. In particular,... 

Bioactive peptides such as superoxide dismutase and interferon arc also hoped to be accumulated in the inflamed and vascular lesions. However, these active peptides cannot be incorporated in lipid microspheres. Instead of incorporating them into lipid microspheres, we devised a method to combine the bioactive peptides with a chemically modified lecithin. In this study, we also examined the tissue distribution of lecithinized IgG. 

Riederer (1990) published a more complex method based on two lipid-like compartments, an acylglycerol lipid compartment and a cuticle compartment. The acylglycerol-air partition coefficient was assumed to equal Kow/Kaw, while measured values of the cuticle-water partition coefficient were employed for the cuticle compartment. Riederer (1995) later modified this model to include a predictive equation for the cuticle-water partition coefficient, based on Kerler and Schonherr s measurements (1988) of eight chemicals with log KqW values ranging from 1.92 to 7.86. They used isolated citrus and rubber plant leaf cuticles as well as tomato and green pepper fruit cuticles. The resulting equation is... 

The composition of protein and lipid in chemically modified keratin fibers was analyzed on silica with chloroform-methanol (80 2, v/v). A rapid immimochromatographic method for the analysis of protein antigens, based tm a sandwich assay format, uses monoclonal antibodies of two distinct specificities, one covalently immobilized to a defined detection zone on a porous membrane, while the other serves as a label. The sample is mixed, and is then passed along the porous membrane by capUlary action, giving a blue color with the antibodies in the detection zone. The detection limit can be below the nanomolar range for the antigen, as in the case of the human chorionic gonadotropin. 

In future, this might be achieved by the introduction of photocleavable linker molecules to remove large residues prior to PCR amplification [175]. Thus, various chemical moieties such as aromatic residues, amino acids or lipid modifications could be introduced in nucleic acid libraries by this method, allowing rapid access to modified libraries for aptamer selection and the selection of novel DNA catalysts. 

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