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Amino acids characteristics

Table II. Molar Ratios of Amino Acids Characteristic of Serum Proteins Compared to Proteins of Other Sources... Table II. Molar Ratios of Amino Acids Characteristic of Serum Proteins Compared to Proteins of Other Sources...
Gelatine Amino acids (characteristic hyd roxy-proline) 9000-70-8 Soluble in hot water, sets to a gel on cooling... [Pg.238]

As the polar mycosides C behave as antigens they must be located in the outer layers of the mycobacterial cell. In fact their external location was demonstrated in M. intracellulare by the use of ferritin-labelled antibodies 214). It has long been known that mycobacteria of the MAIS complex are surrounded by an electron-transparent zone when ultra-thin sections of infected host tissues are examined under the electron microscope. This zone is essentially composed of parallel fibrils wrapped longitudinally around the bacterium. This material was isolated by the use of urea density gradients and analyzed chemically. The three amino acids characteristic of mycosides C and alaninol as well as 6-deoxytalose were identified 194). This material consisted mainly of a mixture of polar and apolar mycosides C, in a ratio about 7 3 (275). [Pg.70]

It is important to be able to determine which chromatography column fractions contain polysaccharides and, specifically, which fractions contain hexosyl, pentosyl, or uronosyl residues. It is also important to detect in the fractions the presence of proteins and the presence of the specific amino acid characteristic of wall proteins, hydroxyproline. The detection of these substances is carried out by facile and sensitive colorimetric procedures. Although these reactions are not discussed here, the most frequently used colorimetric assays in our laboratory are the anthrone assay for detection of hexosyl residues 50), the orcinol assay for detecting pentosyl residues 50), the m-hydroxy-diphenyl assay for detection of uronosyl residues 35), the Lowry assay for detection of proteins 90), and the Kivirikko and Liesmaa assay for the detection of hydroxyprolyl residues 76). [Pg.200]

An alternative approach to peptide sequencing uses a dry method in which the whole sequence is obtained from a mass spectrum, thereby obviating the need for multiple reactions. Mass spec-trometrically, a chain of amino acids breaks down predominantly through cleavage of the amide bonds, similar to the result of chemical hydrolysis. From the mass spectrum, identification of the molecular ion, which gives the total molecular mass, followed by examination of the spectrum for characteristic fragment ions representing successive amino acid residues allows the sequence to be read off in the most favorable cases. [Pg.333]

Organic aromatic molecules are usually sweet, bitter, a combination of these, or tasteless, probably owing to lack of water solubiUty. Most characteristic taste substances, especially salty and sweet, are nonvolatile compounds. Many different types of molecules produce the bitter taste, eg, divalent cations, alkaloids, some amino acids, and denatoirium (14,15). [Pg.11]

The amino acid sequences of hCS-A, hCS-B, and hCS-V are shown in relation to GH in Figure 1. The sequence of hCS-V is predicted from the DNA coding sequence and apparentiy does not possess amino acids 8—55 relative to GH and the other hCS molecules. It is not certain whether hCS-V is expressed or what function it may have. Human CS-A and hCS-B share approximately 85% identity with GH and also possess the disulfide bonds between Cys 53—165 and Cys 182—189 which produce the long and short S—loops characteristic of the PRL/GH family. [Pg.181]

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. [Pg.370]

AH of the protein amino acids are currentiy available commercially and their uses are growing. Amino acids and their analogues have their own characteristic effects in flavoring, nutrition, and pharmacology. [Pg.272]

The dielectric constants of amino acid solutions are very high. Thek ionic dipolar structures confer special vibrational spectra (Raman, k), as well as characteristic properties (specific volumes, specific heats, electrostriction) (34). [Pg.274]

These are the definitions of the two characteristic dissociation constants normally expressed in terms of p K. When three dissociating groups are present in a molecule there are three piC values, ie, pfC, P 3- knowledge of these piC values is important in the separation or isolation of each amino acid by ion-exchange chromatography. [Pg.276]

In many cases only the racemic mixtures of a-amino acids can be obtained through chemical synthesis. Therefore, optical resolution (42) is indispensable to get the optically active L- or D-forms in the production of expensive or uncommon amino acids. The optical resolution of amino acids can be done in two general ways physical or chemical methods which apply the stereospecific properties of amino acids, and biological or enzymatic methods which are based on the characteristic behavior of amino acids in living cells in the presence of enzymes. [Pg.278]

In Foods. Each amino acid has its characteristic taste of sweetness, sourness, saltiness, bitterness, or "umami" as shown in Table 13. Umami taste, which is typically represented by L-glutamic acid salt (and some 5 -nucleotide salts), makes food more palatable and is recognized as a basic taste, independent of the four other classical basic tastes of sweet, sour, salty, and bitter (221). [Pg.296]

Sulfoxides occur widely in small concentrations in plant and animal tissues, eg, aHyl vinyl sulfoxide [81898-53-5] in garlic oil and 2,2 -sulfinylbisethanol [3085-45-8] as fatty esters in the adrenal cortex (1,2). Homologous methyl sulfinyl alkyl isothiocyanates, which are represented by the formula CH3SO(CH2) NCS, where n = 3 [37791-20-1], 4 [4478-93-7], 5 [646-23-1], 8 [75272-81-0], 9 [39036-83-4], or 10 [39036-84-5], have been isolated from a number of mustard oils in which they occur as glucosides (3). Two methylsulfinyl amino acids have also been reported methionine sulfoxide [454-41-1] from cockroaches and the sulfoxide of i -methylcysteine, 3-(methylsulfinyl)alaiiine [4740-94-7]. The latter is the dominant sulfur-containing amino acid in turnips and may account in part for their characteristic odor (4). [Pg.107]

The elemental and vitamin compositions of some representative yeasts are Hsted in Table 1. The principal carbon and energy sources for yeasts are carbohydrates (usually sugars), alcohols, and organic acids, as weU as a few other specific hydrocarbons. Nitrogen is usually suppHed as ammonia, urea, amino acids or oligopeptides. The main essential mineral elements are phosphoms (suppHed as phosphoric acid), and potassium, with smaller amounts of magnesium and trace amounts of copper, zinc, and iron. These requirements are characteristic of all yeasts. The vitamin requirements, however, differ among species. Eor laboratory and many industrial cultures, a commercial yeast extract contains all the required nutrients (see also Mineral nutrients). [Pg.387]


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See also in sourсe #XX -- [ Pg.24 ]




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Acids characteristics

Amino acid sequence evolutionary characteristics

Amino acid spectral characteristics

Amino acids charge characteristics

Amino acids, characteristic frequencies

Amino acids: characteristic chemical

Amino acids: characteristic chemical derivatives

Amino acids: characteristic chemical properties

Amino acids: characteristic chemical structure

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