Translation of "Cysteines" in German

The following substituted cysteines can be obtained in a manner analogous to that described above:

These disulfide bridges are produced between two cysteines.

Suitable thiol derivates are dithiothreitol, monofunctional cysteines, bifunctional peptides, and similar compounds.

For the quantitative and homogeneous alkylation of cysteines the point of time for the modification is crucial.

For the quantitative and homogeneous alkylation of cysteines the position of the modification step in the sample-preparation process is crucial.

Glutathione reduces disulfide bondsformed within cytoplasmic proteins to cysteines by serving as an electron donor.

The peptide contains a total of 12 cysteines which are linked to one another through 6 cystine bridges.

In course of the subsequent irreversible alkylation of the SH groups with iodoacetamide the cysteines are transformed to the stable S-carboxyamidomethylcysteine (CAM; adduct: -CH2-CONH2).

For later use of proteins for protein sequencing, the gels are often prepared the day before electrophoresis to reduce reactions of unpolymerised acrylamide with cysteines in proteins.

All the other constituents in the factor XIII-containing solution which are unable to interact with the matrix, whether because they themselves contain no cysteines or else because their mercapto groups have previously been alkylated, are eluted quantitatively, and in the case of factor XIII from plasma also the "b" subunits which have been separated from the a subunit by treatment with calcium or magnesium.

A variant of the determination procedure is based on the use of labelled polypeptides as labelled receptors which consist of a maximum of 50 amino acid residues and which contain the amino acid sequence ##STR7## preferably CAFRZVC, whereby in each case both cysteines (C) of these amino acid sequences are cyclized to cystine bridges and the polypeptide is monomeric.

Because the "b" subunits themselves do not have free mercapto groups, on the contrary all the SH groups provided by cysteines being in the form of disulfide bonds within the "b" subunits, they do not bind to the carrier matrix and can be removed by washing.

Functional regions or sections or fragments are particularly preferred which contain at least the region of the seven conserved cysteines.

Such hypoallergenic fragments or point mutants of the cysteines can be employed as preparations for the hyposensitisation of allergy sufferers since they react with equal effectiveness with the T-cells, but, owing to the reduced or entirely absent IgE reactivity, result in reduced IgE-mediated side effects.

The table lists the specific proteins (R. commune Secreted Protein, RcSP) with size (AA), length of signal peptide (SP) and number of cysteines (Cys).

Furthermore, both the number and also the surrounding sequence regions of the cysteines of the group 1 allergens of the Poaceae are preserved.

The elements directly modified are the so-called SH groups, molecular appendages comprising sulphur and hydrogen which are typical of cysteines.

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Thanks to sophisticated techniques, the team was finally able to correctly attach the individual fragments, fold the enzyme into its natural form, and correctly couple the cysteines into disulfide bridges to form a functional RNase C.