Dimethylsuberimidate

Hassell, J., and Hand, A. (1974) Tissue fixation with diimidoesters as an alternative to aldehydes. I. Comparison of cross-linking and ultrastructure obtained with dimethylsuberimidate and glutaraldehyde./. Histochem. Cytochem. 22, 223-239. 

The histone octamer of nucleosome core particles was cross-linked by dimethylsuberimidate and isolated from the DNA by precipitation in 3 M NaCl (0.05 M sodium phosphate buffer, pH 7.0). The cross-linked octamer, dissolved at low ionic strength, was reconstituted by mixing with DNA at 1.0 M NaCl (pH 8.0 Tris buffer) and dialyzed against 0.6 M NaCl in the same buffer. The reconstituted particle had properties similar to those of the cross-linked core particle. It sedi-... 

Bifunctional imidoesters such as dimethylsuberimidate may be used to establish whether or not two different proteins or subunits are close together in a complex or in a supramolecular structure such as a membrane or ribosome. 

Dimethylarsine 876 Dimethylglutaric acid, pK 1 value of 99 Dimethylimidazole 868s Dimethylsuberimidate 125s... 

Dansylchloride reacts with amino, thiol, imidazole, phenolic and hydroxy groups. In general, the reaction with aliphatic hydroxyl groups is very slow. This reagent is used widely to detect very small amounts of protein by means of the intense fluorescence of the sulfonamide formed when dansyl chloride reacts with the terminal amino group of protein Dimethylsuberimidate. HCl (1,8- C)... 

Homofimctional cross-linkers have two of the same functional groups. Popular homoftmc-tional cross-linkers are bisimidates (e.g., dimethylsuberimidate) and the N-hydroxy-succinimidesters (e.g., EGS) (Figure 2.27). Many experimenters use dimethylsuberimidate to cross-link protein and peptide ligands. 

Figure 1. Analysis of Mengo capsid protein complexes formed by the crosslinking reagent dimethylsuberimidate (DMS). H-amino acid-labeled virions were incubated with 20 DMS at room temperature for 24 hr, then disrupted by boiling in 2 sodium dodecylsulfate. Capsid proteins and higher-molecular weight complexes were separated by electrophoresis in SDS-containing polyacrylamide gels (60).

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