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Sucrose from amino acids

Fig. 15.11 Factors affecting pH after a 10% glucose or sucrose mouth rinse. Dashed line indicates pH 7. Vectors 1 and 4 increase the pH vectors 2 and 3 decrease the pH. The short-chain carboxylic acids (SCCA) may be produced from amino acids along with ammonia, or from the catabolism of lactic acid (see text and also Fig. 1.8). (From Fig. 9 in Kleinberg I, 2002. A mixed-bacterial ecological approach to understanding the role of the oral bacteria in dental caries causation an alternative to Streptococcus mutans and the specific-plaque hypothesis. Crit Rev Oral Biol Med 13 108-125)... Fig. 15.11 Factors affecting pH after a 10% glucose or sucrose mouth rinse. Dashed line indicates pH 7. Vectors 1 and 4 increase the pH vectors 2 and 3 decrease the pH. The short-chain carboxylic acids (SCCA) may be produced from amino acids along with ammonia, or from the catabolism of lactic acid (see text and also Fig. 1.8). (From Fig. 9 in Kleinberg I, 2002. A mixed-bacterial ecological approach to understanding the role of the oral bacteria in dental caries causation an alternative to Streptococcus mutans and the specific-plaque hypothesis. Crit Rev Oral Biol Med 13 108-125)...
Potential consumer benefits from biotechnology (56) are cost and quaUty. The use of biotech means to increase the level of various sulfur-containing amino acids in coffee proteins, and to enhance sucrose and oil levels, could have an impact on the flavor and aroma of the finished ground coffee product. Also, caffeine level modification/elimination through genetic manipulations of the coffee plant could yield low caffeine coffee without additional processing by the manufacturer. [Pg.390]

An important consequence of sucrose degradation is the development of color from degradation products. Kuridis and Mauch60 have developed an equation for the prediction of color development in model sucrose solutions. Color development was expressed as a function of temperature (90 to 120°C), time (0 to 80 min), pH (7.5 to 9.5), and composition of the solution (sucrose 20 to 60%, invert sugar 0.02 to 0.18%, and amino acids 1 to 3 g/L). The authors claimed, with caution, that the effects of an intended alteration in a unit process in the refinery can be predicted in advance. [Pg.462]

Freeze-drying is a relatively gentle way of removing water from proteins in solution. However, this process can promote the inactivation of some protein types, and specific excipients (cryopro-tectants) are usually added to the product in order to minimize such inactivation. Commonly used cryoprotectants include carbohydrates (such as glucose and sucrose), proteins (such as HSA), and amino acids (such as lysine, arginine or glutamic acid). Alcohols/polyols have also found some application as cryoprotectants. [Pg.168]

Keratinocyte growth factor is a 140 amino acid, 16.3 kDa member of the FGF family. It differs from native keratinocyte growth factor in that the first 23 N-terminal amino acids have been deleted, which improves its stability. After cell growth the product is recovered and purified by a multistep chromatographic protocol. It is presented in lyophilized format in single-use vials and containing mannitol, sucrose, polysorbate 20 and histidine as excipients. It is administered by daily i.v. injection, usually for several days. [Pg.285]

Fig. 2. NAPI facilitates H2A, H2B release from nucleosomes that are on positively coiled DNA (A) but not negatively coiled DNA (B). The positively coiled DNA (6.0 kb) with a superhelical density of + 0.05 and negatively coiled DNA (6.0 kb) with a superhelical density of -0.05 were reconstituted with lysine, arginine-labeled histones H3, H4, H2A, H2B by NaCl dialysis from 2.0 M to 1.2 M to 0.6 M to 0.1 M NaCl over a 14 h period. The samples were incubated with NAPI at 35 °C for 5 min and applied to a 5-20% sucrose/100 mM NaCl/40 mM Tris, pH 7.8 gradient. After sedimentation at 200,000 X g for 5 h, fractions were collected and the distribution of DNA (bottom panel) was determined on agarose gel and the distribution of protein (top panel) on SDS-PAGE followed by fluorography. These data are unpublished observations (V. Levchenko and V. Jackson). The deg-H2A is degraded H2A in which a 15 amino acid peptide of the C terminal has been proteolytically removed. When H2A, H2B is no longer present in a nucleosome, the C terminal region is sensitive to proteolysis [126] from a protease which is a minor contaminate in the NAPI preparation. Fig. 2. NAPI facilitates H2A, H2B release from nucleosomes that are on positively coiled DNA (A) but not negatively coiled DNA (B). The positively coiled DNA (6.0 kb) with a superhelical density of + 0.05 and negatively coiled DNA (6.0 kb) with a superhelical density of -0.05 were reconstituted with lysine, arginine-labeled histones H3, H4, H2A, H2B by NaCl dialysis from 2.0 M to 1.2 M to 0.6 M to 0.1 M NaCl over a 14 h period. The samples were incubated with NAPI at 35 °C for 5 min and applied to a 5-20% sucrose/100 mM NaCl/40 mM Tris, pH 7.8 gradient. After sedimentation at 200,000 X g for 5 h, fractions were collected and the distribution of DNA (bottom panel) was determined on agarose gel and the distribution of protein (top panel) on SDS-PAGE followed by fluorography. These data are unpublished observations (V. Levchenko and V. Jackson). The deg-H2A is degraded H2A in which a 15 amino acid peptide of the C terminal has been proteolytically removed. When H2A, H2B is no longer present in a nucleosome, the C terminal region is sensitive to proteolysis [126] from a protease which is a minor contaminate in the NAPI preparation.

See other pages where Sucrose from amino acids is mentioned: [Pg.119]    [Pg.162]    [Pg.1271]    [Pg.458]    [Pg.156]    [Pg.268]    [Pg.146]    [Pg.184]    [Pg.416]    [Pg.1697]    [Pg.588]    [Pg.300]    [Pg.441]    [Pg.285]    [Pg.5]    [Pg.27]    [Pg.386]    [Pg.119]    [Pg.852]    [Pg.852]    [Pg.91]    [Pg.74]    [Pg.117]    [Pg.183]    [Pg.126]    [Pg.141]    [Pg.232]    [Pg.211]    [Pg.115]    [Pg.116]    [Pg.121]    [Pg.67]    [Pg.66]    [Pg.21]    [Pg.286]    [Pg.248]    [Pg.160]    [Pg.612]    [Pg.193]    [Pg.201]    [Pg.204]    [Pg.492]    [Pg.224]   
See also in sourсe #XX -- [ Pg.222 ]




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