Oriental protein content

The wide angle x-ray diffraction pattern of undeformed corneum exhibits diffuse halos at 4.6 A and 9.8 A common to proteins (Figure 4). The lack of the 5.1-A reflection characteristic of alpha-keratin structures in undeformed comeum suggests that the protein is considerably less oriented and perhaps of a lower alpha content than wool. This is supported by the fact that the 5.1-A reflection begins to appear in samples of comeum which were hydrated and stretched to 100% or more (Figure 6) and allowed to dry in the extended state. The increased orientation of the lipid reflections in the stretched sample demonstrates further their association with the orienting protein fibrils. 

In Asia, oriental noodles play an important role in the diet. Similar to pasta products, oriental noodles manufactured from wheat flours are considered an important source of calories. Practically all the caloric load is supplied by starch and gluten proteins. Alkali noodles contain significant amounts of potassium carbonates, bicarbonates, and phosphates used to impart typical flavors, aroma, texture, and colors. These salts increase sodium, phosphorus, and potassium levels. Wonton or egg noodles contain higher protein content, quality, and overall nutritional value due to the addition of whole eggs. 

GA is well recognized as emulsifier used in essential oil and flavor industries. Randall et al., 1998, reported that the AGP complex is the main component responsible for GA ability to stabilize emulsions, by the association of the AGP amphiphilic protein component with the surface of oil droplets, while the hydrophilic carbohydrate fraction is oriented toward the aqueous phase, preventing aggregation of the droplets by electrostatic repulsion. However, only 1-2% of the gum is absorbed into the oil-water interface and participates in the emulsification thus, over 12% of GA content is required to stabilize emulsions with 20%... 

Although anosmias to these compounds occur at similar levels, some communicative value may arise from the persistence of signal emissions which are not enantiomerically pure (Carman, 1993 Wysocki et al., 1999). In secreted mixtures, the alternate versions of such compounds are produced in a constant ratio since they have identical volatility and hence provide stable informational content to the receiver. Support for this idea comes from the results of the NMR mapping of the BT binding site within the MUP1 carrier (Zidek et al., 1999). Here the protein-ligand complex does exist in the expected ratio, and for both enantiomers, although the orientation of the bound thiazole was interpreted as opposite to that indicated by previous X-ray analyses. 

Abstract To understand how membrane-active peptides (MAPs) function in vivo, it is essential to obtain structural information about them in their membrane-bound state. Most biophysical approaches rely on the use of bilayers prepared from synthetic phospholipids, i.e. artificial model membranes. A particularly successful structural method is solid-state NMR, which makes use of macroscopically oriented lipid bilayers to study selectively isotope-labelled peptides. Native biomembranes, however, have a far more complex lipid composition and a significant non-lipidic content (protein and carbohydrate). Model membranes, therefore, are not really adequate to address questions concerning for example the selectivity of these membranolytic peptides against prokaryotic vs eukaryotic cells, their varying activities against different bacterial strains, or other related biological issues. 

Tofu has long been a source of protein in the Orient. It has much the same importance to the people of the Orient that meats, eggs and cheese have for the people in Western Countries. Tofu is usually sold in the form of a wet cake with a creamy-white color, smooth custard-like texture and a bland taste. It is highly hydrated and, depending on the water content, tofu products with different characteristics can be produced. The typical oriental type of tofu has a water content about 85%. Japanese prefer tofu having a smooth, fragile texture that contains about 88% water. The Chinese, on the other hand, produce many types of firm products with a chewy meatlike texture and a water content as low as 50-60%. Western consumers like tofu with a firm texture therefore, tofu found in the U.S. supermarkets contains 75-80% water. 

The total contents of HAs in broiled, fried, and grilled protein-rich products is generally of the order of several ng per g wet weight (Bartoszek, 2002 Belitz et ah, 2001 Gangolli, 1986). In fried fish fiber (a popular oriental commodity prepared by frying cooked, pressed, and shredded fish meat with... 

For high-performance lAC, the preferred solid support is a glass bead solid support coated wilh either protein-A or protein-A covalently linked with the antibody through a carbodiimide bond (165, 166). In either case, protein-A binds to the Fc portion of the antibody so that the combining sites are oriented to the mobile phase. Once the protein is attached, the lAC matrix is packed into the column either as a slurry or dry. Pump-slurry techniques use buffers with a low salt content, such as Tris or 0.01 M phosphate buffer to minimize friction and denaturation of the immobilized antibody (16). If the solid support consists of glass beads, the packing can be freeze-dried after antibody attachment and packed dry. 

After adsorption one side of the protein molecule is oriented towards the sorbent surface, turned away from the aqueous solution. As a consequence, hydrophobic parts of the protein that are buried in the interior of the dissolved molecule may become exposed to the sorbent surface where they are still shielded from contact with water. Because hydrophobic interaction between apolar amino acid residues in the protein s interior support the formation of secondary structures as a-helices and P-sheets, a reduction of this interaction destabilizes such structures. Breakdown of the a-helices and/or P-sheets content is, indeed, expected to occur if peptide units released from these ordered structures can form hydrogen bonds with the sorbent surface. This is the case for polar surfaces such as oxides, e.g. silica and metal oxides, and with sorbent retaining residual water at their surfaces. Then the decrease in ordered secondary structures leads to an increased conformational entropy of the protein. This may favour the protein adsorption process considerably.13 It may be understood that proteins having an intrinsically low structural stability are more prone to undergo adsorption-induced structural changes. 

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