alpha-chymotrypsin has been researched along with 2-nitro-5-thiocyanobenzoic-acid* in 3 studies
3 other study(ies) available for alpha-chymotrypsin and 2-nitro-5-thiocyanobenzoic-acid
| Article | Year |
|---|---|
Site specificity in vimentin-membrane interactions: intermediate filament subunits associate with the plasma membrane via their head domains.
Fragments of vimentin, generated by chemical or enzymatic cleavages, were analyzed for their capacity to bind to human inverted erythrocyte membrane vesicles. Only peptides comprising the amino-terminal head domain of vimentin molecules were competent in associating with the membranes. In vitro studies also demonstrated that isolated ankyrin (the major vimentin acceptor site on the membrane) binds to an oligomeric species of vimentin and prevents the formation of characteristic 10-nm filaments. These data, taken together with the observation that the NH2-terminal end of vimentin is implicated in the polymerization process (Traub, P., and C. Vorgias, J. Cell Sci., 1983, 63:43-67), imply that intermediate filaments may contact the membrane in an end-on fashion, using the exposed head domains of their terminal subunits. Topics: Animals; Ankyrins; Cattle; Chymotrypsin; Cytoskeleton; Humans; Macromolecular Substances; Membrane Proteins; Microscopy, Electron; Molecular Weight; Peptide Fragments; Thiocyanates; Vimentin | 1985 |
Stoichiometry of microtubule-associated protein (MAP2):tubulin and the localisation of the phosphorylation and cysteine residues along the MAP2 primary sequence.
The stoichiometry of the dimer between microtubule-associated protein 2 (MAP2) and tubulin has been determined by quantitative dodecylsulphate/polyacrylamide gel electrophoresis to be 1:12 mol X mol-1, a value equal to the number of phosphorylation sites that can be labelled in vitro. The distribution of these sites along the MAP2 primary sequence has been determined by cleaving pre-labelled MAP2 with either alpha-chymotrypsin or at the five cysteine residues with nitrothiocyanobenzoic acid. The phosphorylation sites lie in two clusters: ten within the known tubulin-binding domain at one end of the primary sequence, and a pair midway along the sequence. It is postulated that the tertiary structure of MAP2 is folded to bring all twelve sites into association with the twelve tubulin dimers. Topics: Amino Acid Sequence; Animals; Binding Sites; Brain Chemistry; Chemical Phenomena; Chemistry; Chickens; Chymotrypsin; Cysteine; Electrophoresis, Polyacrylamide Gel; Microtubule-Associated Proteins; Phosphorylation; Protein Binding; Protein Kinases; Proteins; Thiocyanates; Tubulin | 1984 |
Cyanylation and cleavage of myosin heavy chains at reactive thiol groups: direct localization of thiol-1 and thiol-2 groups.
Topics: Adenosine Triphosphatases; Animals; Chymotrypsin; Molecular Weight; Muscles; Myosins; Peptide Fragments; Rabbits; Sulfhydryl Compounds; Sulfhydryl Reagents; Thiocyanates | 1981 |