BNPS-SKATOLE
BNPS-SKATOLE structure
|
Common Name | BNPS-SKATOLE | ||
|---|---|---|---|---|
| CAS Number | 27933-36-4 | Molecular Weight | 363.22900 | |
| Density | 1.57 g/cm3 | Boiling Point | 448.8ºC at 760 mmHg | |
| Molecular Formula | C15H11BrN2O2S | Melting Point | 97-100ºC | |
| MSDS | Chinese USA | Flash Point | 225.2ºC | |
|
Chemical cleavage of bovine beta-lactoglobulin by BNPS-skatole for preparative purposes: comparative study of hydrolytic procedures and peptide characterization.
J. Protein Chem. 18(1) , 1-12, (1999) A comparative study of various procedures for tryptophanyl peptide bond cleavage by BNPS-skatole [2-(2-nitrophenyl)-3-methyl-3-bromoindolenine] was carried out on native and on reduced and alkylated bovine beta-lactoglobulin (BLG). The reaction yield and the ... |
|
|
The lobster carapace carotenoprotein, alpha-crustacyanin. A possible role for tryptophan in the bathochromic spectral shift of protein-bound astaxanthin.
Biochem. J. 274 ( Pt 1) , 79-83, (1991) Crustacyanin, cross-linked with dimethyl pimelimidate to stabilize the protein against denaturation, was used to test the effects of tryptophan modification with BNPS-skatole [3-bromo-3-methyl-2-(nitrophenylmercaptol)-3H-indole] on the ability of the apoprote... |
|
|
Interaction of two complementary fragments of the bovine spinal cord myelin basic protein with phospholipid bilayers. An ESR spin-label study.
Biochemistry 28(25) , 9692-8, (1989) The myelin basic protein (MBP) from bovine spinal cord was cleaved at the single tryptophan residue to produce an N-terminal fragment (F1) of molecular weight 12.6K and a C-terminal fragment (F2) of molecular weight 5.8K. The interactions of the two fragments... |
|
|
Photoaffinity labeling of human serum vitamin D binding protein and chemical cleavages of the labeled protein: identification of an 11.5-kDa peptide containing the putative 25-hydroxyvitamin D3 binding site.
Biochemistry 30(30) , 7638-42, (1991) In this paper, we describe photoaffinity labeling and related studies of human serum vitamin D binding protein (hDBP) with 25-hydroxyvitamin D3 3 beta-3'-[N-(4-azido-2-nitrophenyl)amino]propyl ether (25-ANE) and its radiolabeled counterpart, i.e., 25-hydroxyv... |
|
|
Applications of chemical cleavage procedures to the peptide mapping of neurofilament triplet protein bands in sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
Anal. Biochem. 154(1) , 171-82, (1986) A procedure for examining possible sequence homology in the triplet neurofilament proteins using a sodium dodecyl sulfate-polyacrylamide gel electrophoresis system is described. Five different chemical reagents (cyanogen bromide, BNPS-skatole, hydroxylamine, ... |
|
|
Roles of the structure and orientation of ligands and ligand mimics inside the ligand-binding pocket of the vitamin D-binding protein.
Biochemistry 36(24) , 7432-6, (1997) 1alpha,25-Dihydroxyvitamin D3, the vitamin D hormone, manifests its diverse biological properties by specifically binding to the vitamin D sterol-binding pockets of vitamin D-binding protein (DBP) and vitamin D receptor. In the past, several affinity, photoaf... |
|
|
Molecular modeling, affinity labeling, and site-directed mutagenesis define the key points of interaction between the ligand-binding domain of the vitamin D nuclear receptor and 1 alpha,25-dihydroxyvitamin D3.
Biochemistry 39(40) , 12162-71, (2000) We have combined molecular modeling and classical structure-function techniques to define the interactions between the ligand-binding domain (LBD) of the vitamin D nuclear receptor (VDR) and its natural ligand, 1alpha,25-dihydroxyvitamin D(3) [1alpha,25-(OH)(... |
|
|
Probing the vitamin D sterol-binding pocket of human vitamin D-binding protein with bromoacetate affinity labeling reagents containing the affinity probe at C-3, C-6, C-11, and C-19 positions of parent vitamin D sterols.
Arch. Biochem. Biophys. 373(2) , 471-8, (2000) The multiple physiological properties of vitamin D-binding protein (DBP) include organ-specific transportation of vitamin D(3) and its metabolites, manifested by its ability to bind vitamin D sterols with high affinity. In the present investigation we probed ... |
|
|
A comparison of the dodecyl sulfate-induced precipitation of the myelin basic protein with other water-soluble proteins.
Neurochem. Res. 11(2) , 299-315, (1986) The interactions of sodium dodecyl sulfate with a number of proteins were examined at a variety of pH values ranging from 4.8 to 11.6. The dodecyl sulfate-induced precipitation of some of these proteins was observed within a relatively limited range of total ... |
|
|
Photoaffinity labeling identifies the substrate-binding site of mammalian squalene epoxidase.
Biochem. Biophys. Res. Commun. 315(1) , 1-9, (2004) Squalene epoxidase (SE) catalyzes the conversion of squalene to (3S)-2,3-oxidosqualene. Photolabeling and site-directed mutagenesis were performed on recombinant rat SE (rrSE) in order to identify the location of the substrate-binding site and the roles of ke... |