Sort   by:  
 Page size 
Chymotrypsin is widely used in shotgun proteomics owing to its orthogonal cleavage specificity relative to trypsin, which enhances sequence coverage of hydrophobic protein regions. However, commercial preparations often display variable cleavage specificity, trypsin contamination, and elevated misse...
ORGANISM(S): Homo sapiens (Human) 
2026-06-08 | PXD072165 | Pride
Members of the serpin (serine protease inhibitor) superfamily have been identified in higher, multicellular eukaryotes, as well as in bacteria, although surveillance of available genome sequences indicates that bacterial serpin-encoding (ser) homologs are not widely distributed. In members of the ge...
ORGANISM(S): Bifidobacterium breve 
Chymotrypsin-like elastase 1 (CELA1) is a serine protease that is neutralized by alpha-1 antitrypsin (AAT) and prevents emphysema in a murine antisense oligonucleotide model of AAT-deficient emphysema. We tested the role of CELA1 in emphysema development in this genetic model of AAT-deficiency follo...
ORGANISM(S): Mus Musculus (ncbitaxon:10090) 
2023-02-20 | MSV000091330 | MassIVE
Native metabolomics method validation for chymotrypsin. 1. Limit of detection Mollasamide- Chymotrypsin 2. Flowinjection of Mollasamide over UHPLC gradients (with make-up). 3. Binding tests with chymotrypsin and different standards.
ORGANISM(S): Rivularia (ncbitaxon:373984) 
2021-12-18 | MSV000088586 | MassIVE
Machine-learning prediction of affinity and epistasis in the bovine pancreatic trypsin inhibitor–chymotrypsin complex
The 11S globulin legumin typically accounts for approximately 3% of total protein in common bean (Phaseolus vulgaris). It was previously reported that a legumin peptide of approximately 20 kDa is resistant to pepsin digestion. Sequence prediction suggested that the pepsin resistant peptide is locate...
ORGANISM(S): Phaseolus vulgaris (Kidney bean) (French bean) 
2024-08-09 | PXD046332 | Pride
LC-MS/MS analysis of N-linked glycopeptides on Eogt using chymotrypsin
ORGANISM(S): Mus Musculus (mouse) 
Protein–protein interactions (PPIs) are shaped by evolutionary pressures that fine-tune binding affinities and drive the epistatic relationships that support functional outcomes. Here, we used the complex of bovine pancreatic trypsin inhibitor (BPTI) and chymotrypsin as a model system to study how m...
ORGANISM(S): Saccharomyces cerevisiae 
2026-03-28 | GSE325790 | GEO
Chymotrypsin PICS2 with E coli tryptic proteome-derived peptide library
ORGANISM(S): Escherichia Coli (ncbitaxon:562) 
2023-02-11 | MSV000091267 | MassIVE
Sort   by:  
 Page size