Proteins anhydrous

Milk composition expressed in terms of the contents of water (or total solids = 100 - water), fat, protein, lactose, and ash is called gross composition. Protein is often calculated as crude protein by multiplying total N by 6.38, but sometimes it is corrected to true protein 6.38 (TN -NPN) in a few studies, casein and whey protein have been calculated separately. Lactose should be expressed on an anyhydrous basis, but as pointed out previously, this has not always been done. For bovine milk the sum of fat, true protein, anhydrous lactose, and ash would be expected to fall about 0.2-0.3 percentage units short of the total solids contents because of the materials (citrate, NPN, and mis-... 

Amino-1-butanol Amisoft CT-12 Amisoft GS-11 Amisoft HS-11P Amisoft LT-12 Ammonium acrylates/acrylonitro-gens copolymer Ammonium dt ecyl-benzene sulfonate Ammonium isostearate Ammonium laureth-12 sulfate Ammonium nonoxynol-4 sulfate Ammonium oleate Ammonium stearate Ammonium tallate AMMONYX 4 AMM-ONYX 4B AMMONYX CETAC AMMONYX CETAC-30 AMMONYX MO AMMONYX SO AMPD-isostearoyl hydrolyzed collagen AMPD-rosin hydrolyzed collagen Amphisol K Amphisol AMP-isostearoyl hydrolyzed soy protein AMP isostearoyl hydrolyzed wheat protein Anhydrous Lanolin Grade 1 Anhydrous Lanolin Grade 2 Anhydrous Lanolin P.80 Anhydrous Lanolin P95 RA Anhydrous Lanolin P95 Anhydrous Lanolin Superfine Animal GMS Animal Stearic Acid Antarox 17-R-2 Antarox 17-R-4 Antarox 25-R-2 Antarox 31-R-1 Apricot kernel oil PEG-... 

The crospovidones are easily compressed when anhydrous but readily regain their form upon exposure to moisture. This is an ideal situation for use in pharmaceutical tablet disintegration and they have found commercial appHcation in this technology. PVP strongly interacts with polyphenols, the crospovidones can readily remove them from beer, preventing subsequent interaction with beer proteins and the resulting formation of haze. The resin can be recovered and regenerated with dilute caustic. 

However, in most cases enzymes show lower activity in organic media than in water. This behavior has been ascribed to different causes such as diffusional limitations, high saturating substrate concentrations, restricted protein flexibility, low stabilization of the enzyme-substrate intermediate, partial enzyme denaturation by lyophilization that becomes irreversible in anhydrous organic media, and, last but not least, nonoptimal hydration of the biocatalyst [12d]. Numerous methods have been developed to activate enzymes for optimal use in organic media [13]. 

Combination of the Perrin function, p often referred as the frictional ratio due to shape with the frictional ratio (f/fo) enables the degree of expansion of the molecule (vh/ w ) to be estimated, where Vh, (cw / g) is the volume of the swollen molecule (Polysaccharide or protein + associated solvent) per unit mass of polysaccharide and v is the partial specific volume (essentially the anhydrous molecule) ... 

After heating at 40° C, liquid anhydrous milk fat (1 v) and the different protein solutions (10 v) were premixed using a polytron (PT 3000, Kinematica) and emulsified with a homogenizer (ALMO, Legrand, France) at about 40°C in order to obtain oil-in-water emulsions. After separation from the aqueous phase by centrifugation for 5 min at lOOOg, milk fat droplets stabilized by different proteins were washed twice with a phos-... 

There have been no comprehensive studies of how exposure to ethanol, xylene, or paraffin affects proteins following their treatment with aqueous formaldehyde. However, in a related study, Rait et al.25 examined the effect of ethanol incubation on 2 -deoxyadenosine that had been treated with aqueous formaldehyde. Mass spectrometry revealed the presence of N6-ethoxymethyl adducts in addition to hydroxymethyl adducts. This lead to the suggestion that tissue dehydration can result in molecular dehydration, transforming hydroxymethyl groups into Schiff-bases. In such a scheme, the bulk anhydrous ethanol acts as a medium to effectively absorb the water of the... 

Wash the activated particles 3 times with anhydrous THF to remove excess CDI and reaction by-products. After the final wash, remove the solvent and perform a quick wash with ice-cold water to remove most traces of solvent in the particle pellet. Finally, resuspend the particles at 10 mg/ml in cold 0.1 M sodium phosphate, pH 8.2, or 0.1 M sodium carbonate, pH 9.5 (coupling buffer). The higher pH coupling buffer will result in greater reactivity of the imidazole carbamate and greater coupling yields for proteins. 

K Narita. Reaction of anhydrous formic acid with proteins. J Am Chem Soc 81, 1751, 1959. 

Formulation Aranesp is formulated as a sterile, colorless, preservative-free protein solution for intravenous (IV) or subcutaneous (SC) administration. There are two formulations the polysorbate solution includes excipients such as polysorbate 80, sodium phosphate monobasic monohydrate, sodium phosphate dibasic anhydrous, and sodium chloride in water-for-injection while the albumin solution contains albumin, sodium phosphate monobasic monohydrate, sodium phosphate dibasic anhydrous, and sodium chloride in water-for-injection. The pH for both formulations is 6.2 + 0.2. 

The length-distribution studies were recently extended to include an estimate of the radii of gyration of the protein in situ (Ramakrishnan et ai, 1981). The constraint used was that the proteins must have a radius of gyration greater than that of an anhydrous sphere. From their results Ramakrishnan to/. (1981) conclude that only SI and S4 show signs of an extended conformation in situ, whereas 12 proteins (S3, S5, S6, S7, S8, S9, SIO, Sll, S12, S14, S15, and S18) appear quite compact and globular. However, the experimental errors of these estimations are very large. 

Anhydrous acetone is essential, since a water content above 5% decreases the protein yield by precipitation. 

Nakahara Y, Kimura K, friokuchi H, Yagi T (1979) Electrical conductivity of solid state proteins simple proteins and cytochrome C3 as anhydrous film. Chem Lett 8 877-880... 

It is commonly agreed that enzymes are inactive in nearly anhydrous dimethyl sulfoxide (DMSO) [55] and that such inactivity might be a direct result of protein solubilization in the organic milieu, which causes deleterious changes in the proteins secondary and tertiary structures [56]. However, different authors have recently reported that some proteases, namely thermolysin (from Bacillus thermo-proteolyticus) and Proleather (from Bacillus subtilis), were still active in pure DMSO, despite the fact that proteins were indeed solubilized. The former enzyme cata-... 

Refining. After saccharification, the hydrolyzate is clarified by precoat filtration, or possibly membrane filtration, to remove traces of insoluble fat, protein, and starch. Treatment with powdered carbon, granular carbon, and/or ion-exchange resins is then used to remove residual trace impurities, color, and inorganic constituents. The refined hydrolyzate can be dried to a solid product, evaporated to a high dextrose syrup, or processed to crystalline monohydrate or anhydrous dextrose. A typical process for production of crystalline dextrose is shown in Figure 2(7). 

The extent of succinylation and acetylation was determined by the trinitrobenzenesulfonic acid (TNBS) method as described by Hall et al. (31) Protein (5 mg) isolated from chemically modified and control soy flour in 0.8 ml of aqueous solution was added to 1 ml of 4% NaHCOg, followed by addition of 0.2 ml of 2,4,6-trinitrobenzenesulfonic acid (12.5 mg/ml). The reaction mixture was incubated at 4O C for 2 hr, and 3.5 ml of 36% HCl was added. The tubes were stoppered and kept at 110 C for 4 hr. After cooling to room temperature (24 C), volume of solution was made up to 10 ml with distilled water, and contents were extracted twice with anhydrous diethyl ether. 

Extraction of sulfonamides and diaminopyrimidine potentiators from edible animal products should render the bound residues soluble, remove most or all of the proteins, and provide high yields for all analytes. Sample extraction/deprotei-nization is traditionally accomplished with polar solvents including acidic aqueous solutions (211,214-222), acetonitrile (56,223-232), chloroform (233-240), ethyl acetate (29,241-244), dichloromethane (204,242,245-247), acetone (194, 248, 249), or various combinations of them. Use of dichloromethane at pH 10 in the presence of an ion-pairing reagent (tetrabutylammonium) has also been reported to work extremely well in the extraction of sulfadimethoxine and ormeto-prim residues from catfish muscle (250) and animal tissues (251). Anhydrous sodium sulfate may be added to dehydrate tissue samples to permit better exposure of the matrix to tire solvent. 

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