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Protein-lipid complexes are known to result from complex molecular interactions which contribute to physiochemical and functional properties of foods. To identify the interactions of food proteins with lipids and the associated changes in properties, the following factors were investigated: incubation temperature, pH, type of lipids (phospholipid, triglyceride and fatty acids) and different proteins (ovalbumin and soybean glycinin). The effects of lipids on physiochemical and functional characteristics of ovalbumin and glycinin were investigated using polyacrylamide gel electrophoresis (PAGE), fluorescence, differential scanning calorimetry (DSC), Fourier transform infrared (FTIR) spectroscopy, and emulsification and gelation properties. / The results showed that pH, temperature and the type of lipids affected both ovalbumin-lipid interactions and physiochemical properties of ovalbumin. Changes in the electrophoretic behavior of ovalbumin were related to the presence of lipids, and the relative fluorescence of ovalbumin decreased in the presence of lipids at different pH values. In addition, lipids increased the stability of ovalbumin as revealed by the thermal denaturation (Td) and by the enthalpy transition (DeltaH). FTIR spectra in the amide I absorption region revealed that lipids affected the secondary structure of ovalbumin. Changes in the integrated intensity of the amide II band between (1520--1555) cm -1 in the presence of D2O showed that H-D exchange of ovalbumin decreased in the presence of lipids. Emulsifying properties, gel strength and water holding capacity (WHC) of ovalbumin increased significantly (P < 0.05) in the presence of lipids. Scanning electron microscopy (SEM) showed difference in the microstructure of ovalbumin gel in the presence of different lipids. The more pronounced effect of lipids was observed with lecithin and the lowest was with stearic acid. The order of magnitude for the effects of lipids on physiochemical and functional properties of ovalbumin was: lecithin > cocoa butter > oleic acid > linoleic acid > linolenic acid > stearic acid. It is likely that the degree of polarity of lipids play an important role in protein-lipid interactions and in the enhancement of the functional properties of ovalbumin. / The effects of soybean oil (SO), soybean lecithin (SL) and a mixture of both (SOL) on physiochemical and functional properties of soybean glycinin were studied at pH 8.0, with incubation at 40°C. Changes in the electrophoretic behavior were related to the presence of lipids. Relative fluorescence of glycinin decreased in the presence of lipids. Lipids increased the thermal stability (Td) of glycinin from 89.7°C to 92.0°C, 94.3°C and 93.4°C with SO, SL and SOL respectively. FTIR spectra indicated changes in both; the secondary structure and H-D exchange of glycinin in the presence of lipids. Gel strength, WHC and emulsifying properties of glycinin increased significantly (P < 0.05) in the presence of lipids; the order of consequence increase was: SL > SOL > SO. SEM showed difference in the microstructure of glycinin gels with the different lipids used. Overall, the results demonstrate both quantitative and qualitative effects on the physiochemical and functional properties of ovalbumin and glycinin as a result of protein-lipid interactions.

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Methylglyoxal bis(guanylhydrazone) (MGBG) was incorporated extensively into baby hamster kidney (BHK-21/C13) cells by a temperature - and Na⁺, K⁺ - ATPase linked mechanism. The uptake of the drug was dependent on the growth state of the cells and transformed cells (PyY-cells) incorporated MGBG to a greater extent than normal BHK cells. The uptake of the drug was inhibited by coadministration with spermidine, spermine and N¹-acetylspermine and to a lesser extent by putrescine and Mg²⁺ ions. MGBG and spermine were cytotoxic and both compounds stimulated spermidine acetyltransferase (SAT) activity in BHK cells but not in PyY-cells suggesting that transformation enhanced resistance of the cells.SAT activity was present in both the nuclear and cytosolic compartment of both cell-lines and MGBG stimulation resulted in an increase in both N¹- and N⁸-acetylspermidine production in the nucleus and almost exclusive N¹-acetylspermidine production in the cytosol. MGBG stimulated spermine acetyltransferase activity in both nuclear and cytosolic compartments of mammalian cells. Increased intracellular acetylation after MGBG-treatment resulted in enhanced excretion of putrescine and N¹-acetylspermidine from both BHK- and PyY-cells implicating acetylation as a means to control intracellular polyamine content. MGBG was itself acetylated in the nucleus of both cell-lines, as was putrescine. However, prior MGBG treatment inhibited the acetylation of MGBG itself and the diamine suggesting that the two compounds are acetylated by a common nuclear acetyltransferase.A cytosolic spermidine acetyltransferase enzyme was purified over 2000-fold from BHK-cells and was found to acetylate putrescine, spermidine, spermine and MGBG. The activity of the enzyme preparation to all these compounds suggests that the enzyme preparation contained nuclear acetyltransferase activity. A model is preposed for the role of acetylation in both the nuclear and cytosolic compartments of mammalian cells.

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