Other protein fractions

In addition to the caseins and whey proteins, milk contains two other groups of proteins or protein-like material, i.e. the proteose-peptone fraction and the non-protein nitrogen (NPN) fraction. These fractions were recognized as early as 1938 by Rowland but until recently very little was 

Total nitrogen = Kjeldahl I Casein = Kjeldahl I-Kjeldahl n Non-protein nitrogen = Kjeldahl III 

Proteose peptone N = Kjeldahl IV-Kjeldahl in Serum protein = Kjeldahl II- Kjeldahl IV 

---

Relative to concentrations of other protein fractions in patients with normal cytological and biochemical flndings and in cases with the lymphocytic cytological... 

The glutamine analog 6-diazo-5-oxo-L-norleucine (DON) inhibits L-glu-tamine n-fructose-6-phosphate amidotransferase (Section III) in the-pathway of conversion of C-glucose to both sialic acid and N-acetylga-lactosamine and, as expected, thereby inhibits incorporation of C-glu-cose into OSM. With glucose as the sole carbohydrate source in the incubation medium, DON also inhibits incorporation of radioactive amino acids into OSM but causes a concomitant increased incorporation of labeled amino acid into other protein fractions these latter proteins may contain nonglycosylated polypeptide precursors of OSM. All the inhibitory effects of DON are prevented if glucosamine is present in the incul ition medium. 

The protein fraction is responsible for a major part of membrane function Non polar materials can diffuse through the bilayer from one side to the other relatively eas ily but polar materials particularly metal ions such as Na" K" and Ca " cannot The... 

The high protein flour may be used to fortify or blend with other flours. Recombining some of the high protein fraction with the coarse portions permits a miller to tailor a flour of protein value to a buyer s specifications. 

Casein. Milk contains proteins and essential amino acids lacking in many other foods. Casein is the principal protein in the skimmed milk (nonfat) portion of milk (3—4% of the weight). After it is removed from the Hquid portion of milk, whey remains. Whey can be denatured by heat treatment of 85°C for 15 minutes. Various protein fractions are identified as a-, P-, and y-casein, and 5-lactoglobulin and blood—semm albumin, each having specific characteristics for various uses. Table 21 gives the concentration and composition of milk proteins. 

The numerous separations reported in the literature include surfactants, inorganic ions, enzymes, other proteins, other organics, biological cells, and various other particles and substances. The scale of the systems ranges from the simple Grits test for the presence of surfactants in water, which has been shown to operate by virtue of transient foam fractionation [Lemlich, J. Colloid Interface Sci., 37, 497 (1971)], to the natural adsubble processes that occur on a grand scale in the ocean [Wallace and Duce, Deep Sea Res., 25, 827 (1978)]. For further information see the reviews cited earlier. 

For each fold one searches for the best alignment of the target sequence that would be compatible with the fold the core should comprise hydrophobic residues and polar residues should be on the outside, predicted helical and strand regions should be aligned to corresponding secondary structure elements in the fold, and so on. In order to match a sequence alignment to a fold, Eisenberg developed a rapid method called the 3D profile method. The environment of each residue position in the known 3D structure is characterized on the basis of three properties (1) the area of the side chain that is buried by other protein atoms, (2) the fraction of side chain area that is covered by polar atoms, and (3) the secondary stmcture, which is classified in three states helix, sheet, and coil. The residue positions are rather arbitrarily divided into six classes by properties 1 and 2, which in combination with property 3 yields 18 environmental classes. This classification of environments enables a protein structure to be coded by a sequence in an 18-letter alphabet, in which each letter represents the environmental class of a residue position. 

Plasma protein fractions are used to treat hypovolemic (low blood volume) shock that occurs as the result of bums, trauma, surgery, and infections, or in conditions where shock is not currently present but likely to occur. Plasma protein fractions are also used to treat hypoproteinemia (a deficiency of protein in the blood), as might be seen in patients with nephrotic syndrome and hepatic cirrhosis, as well as other diseases or disorders. As with human pooled plasma, blood type and crossmatch is not needed when plasma protein fractions are given. 

Most IV solutions should not be combined with any other solutions or drug s but should be administered alone The nurse should consult the drug insert or other appropriate sources before combining any drug with any plasma protein fraction. 

Solutions used to manage body fluids are often administered IV. Before administering an IV solution, the nurse assesses the patient s general status, reviews recent laboratory test results (when appropriate), weighs the patient (when appropriate), and takes the vital signs. Blood pressure, pulse, and respiratory rate provide a baseline, which is especially important when the patient is receiving blood plasma, plasma expanders, or plasma protein fractions for shock or other serious disorders. 

There are approximately 200 other proteins present in bone, though most of them are present only in trace amounts (Delmas et al., 1984 Linde et al., 1980, as cited in van Klinken, 1991). The second most common bone protein, osteocalcin, comprises 1-2 weight % of total fresh bone. Osteocalcin bonds with both the bone mineral fraction and bone collagen, but it seems to be unstable in solutions. Due to its small molecular size and strong mineral stabilization, osteocalcin can survive up to 50.000 years (C.l. Smith et al., 2005), and it may offer an alternative to the use of collagen in paleoenvironmental stable isotope research. However, osteocalcin s role and importance in this field of study has yet to be defined (Collins et al., 2002). 

The range of whey products that are used include, for example, ultra-filtered and dried WPC, which contains between 20% and 89% protein ion exchange and membrane filtered WPI, which contains at least 90-95% protein (Tunick, 2008) and other whey fraction-enriched products such as p-lactalbumin. These enriched protein whey products can be texturized and used in the manufacture of high-protein content puffed com products (Onwulata et al, 2010). 

The alkali-soluble protein of the peel of lemons treated with hydrogen sulfide, sulfur dioxide, and sulfuric acid contained radioactive sulfur, but the fruit treated with hydrogen sulfide had a significantly lower per cent specific activity in the alkali-soluble protein fraction than did the sulfur dioxide or sulfuric acid treated fruits (Table VII). These results suggest that sulfur dioxide and sulfuric acid react with protein more directly, while hydrogen sulfide perhaps must be oxidized first, as indicated in Table III. It also appears (from Table VII) that the alkali-soluble protein may have been dismuted as the amounts isolated were less in both the hydrogen sulfide and sulfur dioxide treated fruit than in the incubated or nonincubated controls. Other evidence of dismutation has been obtained in experiments where incubation at 60° C. was accompanied by the production of free ammonia (18), and the recovery of free ammonia and six amino acids in the exudates of incubated and sulfur-dusted fruits (18). 

Apart from its natural occurrence, Co may find its way into other proteins either adventitiously or deliberately. A study was undertaken where the blood, serum, and plasma of workers occupationally exposed to Co were analyzed for the element.1189 When separated by gel electrophoresis under denaturing conditions, the Co fractions in all blood, serum, and plasma samples showed a similar protein pattern. A variety of proteins of differing size were found to bind Co in fractions collected at pFl 5, whereas only hemoglobin was found in the pH 7 fractions. The conclusions were that in vivo Co is bound to plasma proteins, perhaps albumin and hemoglobin. 

As noted above, whole-cell MALDI-TOF MS was intended for rapid taxonomic identification of bacteria. Neither the analysis of specific targeted bacterial proteins, nor the discovery of new proteins, was envisioned as a routine application for which whole cells would be used. An unknown or target protein might not have the abundance or proton affinity to facilitate its detection from such a complex mixture containing literally thousands of other proteins. Thus, for many applications, the analysis of proteins from chromatographically separated fractions remains a more productive approach. From a historical perspective, whole-cell MALDI is a logical extension of MALDI analysis of isolated cellular proteins. After all, purified proteins can be obtained from bacteria after different levels of purification. Differences in method often reflect how much purification is done prior to analysis. With whole-cell MALDI the answer is literally none. Some methods attempt to combine the benefits of the rapid whole cell approach with a minimal level of sample preparation, often based on the analysis of crude fractions rather... 

The ongoing development of top-down protein MS/MS capabilities (MS/MS) should prove quite valuable to researchers looking to identify and characterize proteins fractionated by 2DLC separations. Such methods are currently limited by restrictions on the maximum size of proteins analyzed, as well as analysis time-requirements that limit coupling of these methods with online LC analysis. Investigators from labs, such as Kelleher, McLafferty, Hunt (Coon et al., 2005 Meng et al., 2005 Han et al., 2006), and others are rapidly addressing these issues, and their methods will likely be adopted by many other researchers over the next few years. 

---