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Cystamine may be used to make immunotoxin conjugates by a disulfide interchange reaction. Modification of antibody molecules using an EDC-mediated reaction creates a sulfhydryl-reactive derivative. A-chain toxin subunits containing a free thiol can be coupled to the cystamine-modified antibody to form disulfide crosslinks.

Cystamine PEGDGE PCL hydrogels stained with Hematoxylin and Eosin

Cystathionine levels are increased in human cortex. Levels of cystathionine were measured in cortex from different species and in different human tissues. Data are from TaUan et al.

CYSTEAMINE OXYGENASE ACTIVITY IN HUMAN LIVER 30 mg of human liver homogenate, j tained by biopsy, were incubated, as reported in the text, with S-cysteamine in the presence of cofactor. A zero time, B 4 hours incubation. The radioactive peaks correspond to taurine .

Cystein zwitterion

Cysteine adducts of the sesquiterpene lactone, ele-phantopin .

Cysteine adducts of the sesquiterpene lactone, elephantropin.

Cysteine adducts of the sesquiterpene lactone, parthenin.

Cysteine also may be used in an Ellman s assay to determine the maleimide activation level of SMCC-derivatized proteins. Reaction of the activated carrier with different amounts of cysteine results in various levels of sulfhydryls remaining after the reaction. The coupling must be done in the presence of EDTA to prevent metal-catalyzed oxidation of sulfhydryls. Detection of the remaining thiols using an Ellman s assay indirectly indicates the amount of sulfhydryl uptake into the activated carrier. Comparison of the Ellman s response to the same quantity of cysteine plus an unactivated carrier indicates the absolute amount of sulfhydryl that reacted. Calculation of the maleimide activation level then can be done.

Cysteine and methionine are highly susceptible to oxidation reactions. Cysteine thiols can form disulfide linkages with other cysteine groups or be oxidized to cysteic acid. Methionine is oxidized very easily to the sulfoxide or sulfone products.

Cysteine and serine protease inhibitors for antimalaria screening. Lead compounds were converted into the corresponding probes for target discovery.

Cysteine conformations in kalata Bl. Average dihedral angles in the NMR ensembles, consistent with the dihedral angles determined experimentally by NOE and coupling constants.

Cysteine conjugate jS-lyase bioactivation of cysteine conjugates of haloalkenes.

Cysteine decomposition by a Strecker degradation mechanism formation of H2S

Cysteine is in excess in stable conditions.

Cysteine Knot Core Containing Three Peptide Chains11391 1 Cys

Cysteine ligand environment in A. den. azurin showing the two N-H-S hydrogen bonds. Distances are for the oxidized protein, with those for the rednced form in parentheses. Also shown are the hydrogen bonds made by the conserved Asn 47, which help constrain the copper site

Cysteine ligand environment in A. den. azurin showing the two N-H-S hydrogen bonds. Distances are for the oxidized protein, with those for the reduced form in parentheses. Also shown are the hydrogen bonds made by the conserved Asn 47, which help constrain the copper site

Cysteine linkages in porphyrin c. with that of protoporphyrin IX.

Cysteine oxidation and disulfide bond formation See also

Cysteine oxidation products.

Cysteine positions in the HCIIs. The cysteine positions of HCIIs are placed on a schematic diagram of HCII secondary structure. Helices are shown as rectangles and loops as lines. Experimentally determined and predicted disulfide bond linkages are shown.

Cysteine positions in the sequence of amino acids In mammalian metallothlonelne.

Cysteine protease ABPs. Examples of two of the most commonly used classes of probes that target cysteine proteases. A peptide epoxide based on the natural product E-64 reacts with the active site cysteine to form a stable adduct upon epoxide ring opening. This class of compounds has been used exclusively to target cysteine cathepsins.

Cysteine protease and subtilisin-like protease pathways for proneuropeptide processing. Distinct cysteine protease and subtilisin-like protease pathways have been demonstrated for pro-neuropeptide processing. Recent studies have identified secretory vesicle cathepsin L as an important processing enzyme for the production of the endogenous enkephalin opioid peptide. Preference of cathepsin L to cleave at the NH2-terminal side of dibasic residue processing sites yields peptide intermediates with NH2-terminal residues, which are removed by Arg Lys aminopeptidase. The well-established subtilisin-like protease pathway involves several prohormone convertases . PC1 3 and PC2 have been characterized as neuroendocrine processing proteases. The PC enzymes preferentially cleave at the COOH-terminal side of dibasic processing sites, which results in peptide intermediates with basic residue extensions at their COOH-termini that are removed by carboxypeptidase E H.



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