Disease relevance of EINECS 250-093-9

• A fragment was obtained by treating Clostridium perfringens enterotoxin with 2-nitro-5-thiocyanobenzoic acid, a reagent which specifically cleaves the amino-terminal peptide bond of cysteine residues [1].
• Partial cleavage of synapsin I by collagenase, 2-nitro-5-thiocyanobenzoic acid, and Staphylococcus aureus V8 protease suggests that at least three glycosylation sites exist along the molecule [2].

High impact information on EINECS 250-093-9

• Previous studies using enzymatic digestion, 2-nitro-5-thiocyanobenzoic acid cleavage, and rotary shadowing techniques have placed the spectrin-ankyrin binding site in the COOH-terminal third of beta-spectrin, but the precise site is not known [3].
• Peptide antisera specific for either the amino- or carboxyl-terminal regions of villin were used to locate the position of cysteine residues in immunoblots of villin cleaved with 2-nitro-5-thiocyanobenzoic acid [4].
• Cleavage of protein 4.1 at cysteine residues by 2-nitro-5-thiocyanobenzoic acid produces a series of doublets which differ by approximately 2,000 daltons and have identical peptide maps [5].
• Though DNase does not contain any cysteine residues, incubation of the enzyme with 2-nitro-5-thiocyanobenzoic acid in the presence of Ca2+ at pH values above 7.5 results in an irreversible inactivation of the enzyme [6].
• Since the 7.5-kDa fragment was sensitive to hydrolysis by 2-nitro-5-thiocyanobenzoic acid, we circumscribed the labeling site of 125I-[Sar1,Bpa8]AngII within amino acids 285 and 295 of the AT1 receptor [7].

Biological context of EINECS 250-093-9

• In this study, we produced a monoclonal antibody, Sp316, capable of recognizing the C-terminal region of beta-spectrin regardless of its phosphorylation state and used it to purify the phosphorylated region after 2-nitro-5-thiocyanobenzoic acid cleavage of spectrin [8].
• They indicate no amino acid sequence diversity according to peptide mapping, but differ in their redox state, as shown by free-sulfhydryl-group-specific cleavage at cysteine residues with 2-nitro-5-thiocyanobenzoic acid [9].

Anatomical context of EINECS 250-093-9

• Also, keratan sulphate-depleted and cyanogen bromide (CNBr) and 2-nitro-5-thiocyanobenzoic acid (NTCB)-cleaved PG elicited stronger T cell responses, as they were more easily processed than the native molecule [10].

Associations of EINECS 250-093-9 with other chemical compounds

• Two fragment pools, one of MW greater than 10,000 and the other of MW between 1,000 and 10,000, were prepared by the sequential treatment of rye grass pollen extract with cyanogen bromide (cleavage at Met-X) and 2-nitro-5-thiocyanobenzoic acid (cleavage at X-Cys) [11].
• Specific cleavage of glucosephosphate isomerases at cysteinyl residues using 2-nitro-5-thiocyanobenzoic acid: analyses of peptides eluted from polyacrylamide gels and localization of active site histidyl and lysyl residues [12].
• Four fragments of alpha-tropomyosin were prepared by specific cleavage at the Cys 190 by 2-nitro-5-thiocyanobenzoic acid and by tryptic digestion [13].

Gene context of EINECS 250-093-9

• The epitopes for the individual monoclonal antibodies were mapped to the caldesmon primary structure using chymotryptic and 2-nitro-5-thiocyanatobenzoic acid fragments [14].
• N-terminal sequence analysis indicated that each was contained within one of the 2-nitro-5-thiocyanobenzoic-acid-derived calmodulin-binding fragments.(ABSTRACT TRUNCATED AT 400 WORDS)[15]
• Since it is well known that fibronectin is composed of multiple domains which differ in their biological activities, this study also attempted to clarify which domain(s) inhibit TDF activity, through the use of trypsin, thermolysin and 2-nitro-5-thiocyanobenzoic acid (NTCB) [16].
• Cyanylation of rhodanese by 2-nitro-5-thiocyanobenzoic acid [17].

References