N-epsilon-lithocholyl lysine (NELL) is a component of tissue-bound lithocholic acid (TBL). The isolation of NELL from native protein sources was simulated by hydrolysis of lithocholyl-bovine serum albumin (BSA) (synthesized by coupling lithocholyl-N-hydroxysuccinimide to fatty acid-free BSA) by digestion with a
Evidence for the formation of a novel glutathione conjugate in the metabolism of an aromatic amine derivative.
D H Hutson et al.
Drug metabolism and disposition: the biological fate of chemicals, 12(4), 523-524 (1984-07-01)
Bioscience, biotechnology, and biochemistry, 62(8), 1488-1491 (1998-10-03)
An easy and highly sensitive method for measuring histamine by HPLC analysis coupled with precolumn derivatization was established. The amino group of histamine was completely colorimetrically labelled with 4-N,N-dimethylamino-azobenzene-4'-isothiocyanate (DABITC) in the presence of sodium bicarbonate at 90 degrees C
The Journal of biological chemistry, 264(6), 3111-3115 (1989-02-25)
A new water-soluble color reagent, 4-N,N-dimethylaminoazobenzene-4'-isothiocyano-2'-sulfonic acid (S-DABITC), was used to identify lysine residues of antithrombin III which participate in the binding of heparin. Antithrombin, modified with S-DABITC in the presence and absence of low molecular weight heparin (Mr 5000)
A synthetic peptide analog, with one peptide carbonyl group replaced by a methylene bridge, was submitted to structural analysis by Edman degradation. Multiple cleavages were obtained in the first cycle, due to phenylthiocarbamylation of the internal secondary amine as well
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