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Disulfide bonds, reduction

Fig. 6.22. Folate-FRET sensor structure and its application to measure disulfide bond reduction in endosomes. The molecule contains the folate moiety which is recognized by the folate receptor situated at the plasma membrane. This recognition leads to endocytosis and after some time to cleavage of the probe. [Pg.285]

Scheme 5. Direct labeling of monoconal antibodies by disulfide bond reduction. Scheme 5. Direct labeling of monoconal antibodies by disulfide bond reduction.
THE CELLULAR FUNCTION OF ACROSIN AS A SPERM LYSIN. Acrosin fulfills most of the above listed criteria for a sperm lysin. It has been localized onto both the inner and outer acrosomal membranes by histochemical and immunochemical localization procedures (60.61). and is at the correct place to function in fertilization. Complete ZP dissolution by homologous acrosins, the second lysin criterion, is not observed with all species. With boar acrosin, dissolution of the porcine ZP was never visually observed, as was true with sheep ZP and ram acrosin (62). To visualize the effect of acrosin on the ZP, electrophoretic or other separation procedures that employed denaturants and disulfide bond reduction were required (7.37.38). Complete dissolution of the ZP does not occur in normal fertilization, since the ZP is needed for the continued development of the embryo ... [Pg.218]

Disulfide bonds Reduction Alkaline pH -SH, mispairing Hydrolysis, B elimination... [Pg.10]

Figure 4.26. Disulfide-Bond Reduction. Polypeptides linked by disulfide bonds can be separated by reduction with dithiothreitol followed by alkylation to prevent reformation. Figure 4.26. Disulfide-Bond Reduction. Polypeptides linked by disulfide bonds can be separated by reduction with dithiothreitol followed by alkylation to prevent reformation.
Disulfide (-S-S-) bonds play an important role in the structure and function of proteins. IgG molecules are comprised of two heavy and two light chains linked by interchain disulfide bonds. In addition, intrachain disulfide bonds are also present in IgGs. Alkyl thiols have been used to demonstrate the structural and functional role played by disulfide bonds. Reduction of IgGs with alkyl thiols under denaturing conditions results in separation of light and heavy chains. [Pg.385]

Fig. 17.7. Engineered protein designed for mechanochemistry studies, (a) A pair of cysteine residues introduced into the 127 protein (positions 32 and 75 suifur atoms as spheres) spontaneously form a buried disuifide bond. (b). In response to an unfolding force, the protein extends right up to the disuifide bond. Unfoiding exposes the disulfide bond to the solution, (c) Then, a nucieophiie such as DTT can initiate a Sn2 reaction, leading to the reduction of the disuifide bond and the concomitant extension of the amino acids that were trapped behind the disuifide bond. This sequence of events nnambiguousiy identifies individual disulfide bond reduction events, allowing for the stndy of a pulling force on a Sn2 chemicai reaction... Fig. 17.7. Engineered protein designed for mechanochemistry studies, (a) A pair of cysteine residues introduced into the 127 protein (positions 32 and 75 suifur atoms as spheres) spontaneously form a buried disuifide bond. (b). In response to an unfolding force, the protein extends right up to the disuifide bond. Unfoiding exposes the disulfide bond to the solution, (c) Then, a nucieophiie such as DTT can initiate a Sn2 reaction, leading to the reduction of the disuifide bond and the concomitant extension of the amino acids that were trapped behind the disuifide bond. This sequence of events nnambiguousiy identifies individual disulfide bond reduction events, allowing for the stndy of a pulling force on a Sn2 chemicai reaction...
In order to study the kinetics of disulfide bond reduction as a function of the pulling force, we utilize a double pulse protocol in force clamp. With a first pulse, we unfold the unsequestered region of the (I27s-s)8 modules in the polyprotein, exposing the disulfide bonds to the solution. With a second (test) pulse, we track the rate of reduction of the exposed disulfides at various pulling forces in the presence of various reducing agents. [Pg.324]

Dehydroalanine 116 desmosine 48, 49 diazo compounds 157 aryl diazonium salts, reactive properties 157 synthesis 160 diazoacetates, analysis of products 165 reactive properties 162 synthesis 164 diazoketones, analysis of products 162 conversion to haloketones 139 reactive properties 165 synthesis 140 diazomethane preparation 141 reactive properties 162 diazonium salts 89 diazonium-IH-tetrazole 90, 95 3,4-dihydroxyproline 52, 53 diimidoesters 69 diisopropylfluorophosphate 130 2,3-dimethylmaleic anhydride 83 dinitrophenylation 79 disulfide bond reduction 103... [Pg.202]

Mekalanos JJ, Collier RJ, Romig WR (1979) Enzymatic activity of cholera toxin II. Relationships to proteolytic processing, disulfide bond reduction, and subunit composition. In J. Biol. Chem. 254 5855-5861. [Pg.15]

P-galactosidase also exhibited aggregation via disulfide bond formation at relatively low water content. The participation of disulfide bond formation in this case was confirmed by size-exclusion chromatography. The formed aggregate was not dissociated by guanidine hydrochloride but was dissociated by dithiothreitol, a disulfide bond reductant.811... [Pg.192]

Kuwajima K, Ikeguchi M, Sugawara T, et al. (1990). Kinetics of disulfide bond reduction in a-lactalbumin by dithiothreitol and molecular basis of superreactivity of the cys6-cysl20 disulfide bond. Biochem. 29 8240-8249. [Pg.407]

Wiita AP, Ainavarapu SRK, Huang HH, Fernandez JM (2006) Force-dependent chemical kinetics of disulfide bond reduction observed with single-molecule techniques. Proc Natl... [Pg.29]

Perreault, S. D., Wolff, R. A., and Zirkin, B. R. (1984). The role of disulfide bond reduction during mammalian sperm nuclear decondensation in vivo. Dev. Biol 101, 160-167. [Pg.514]

Compare the oxidized and reduced chemokine spectra to confirm that disulfide bond reduction caused the NMR signals to collapse (Fig. 6, bottom). [Pg.554]

Chromophores can also be synthetically attached to specific protein groups, either to assist identification or incidental to blocking reactive fiinctionalities. One common chromophore is the pyridylethyl group added to cysteine using 4-vinylpyridine after disulfide bond reduction but prior to enzymatic digestion. The pyridylethyl cysteine has a strong absorbance maximum near 254 nm that permits easy on-line identification of Cys-containing peptides [16]. [Pg.753]

Disulfide bond reduction, which might also cause some release of structural constraints imposed by the disulfide bond and protein unfolding at the interface. Soy glycenin, which has limited film-forming properties due to its compact, stable, disulfide-linked structure [128] will be significantly more surface-active when some of its six disulfide-linked acidic and basic subunits have been reduced (Fig. 48). Reduction, oxidation-reduction, or oxidation of the amino acid cysteine to form an open thiol (sulfhydryl) groups. [Pg.354]


See other pages where Disulfide bonds, reduction is mentioned: [Pg.284]    [Pg.737]    [Pg.17]    [Pg.847]    [Pg.194]    [Pg.164]    [Pg.325]    [Pg.327]    [Pg.328]    [Pg.173]    [Pg.296]    [Pg.10]    [Pg.95]    [Pg.26]    [Pg.182]    [Pg.96]    [Pg.281]    [Pg.4]    [Pg.640]    [Pg.238]    [Pg.238]    [Pg.119]    [Pg.296]   
See also in sourсe #XX -- [ Pg.324 ]

See also in sourсe #XX -- [ Pg.253 , Pg.261 , Pg.265 , Pg.267 , Pg.278 , Pg.290 , Pg.291 , Pg.305 , Pg.401 , Pg.434 ]




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Bonds disulfides

Bonds reduction

Disulfide bond reduction and

Disulfide bond reduction, effect

Disulfide bonds

Disulfide bonds reduction/alkylation

Disulfide bonds, reduction inhibitory activity

Disulfide reduction

Disulfides reduction

Insulin disulfide bonds, reduction

Protein disulfide bond reduction

Reduction of the Disulfide Bond

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