isocoumarins has been researched along with alpha-chymotrypsin in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 1 (25.00) | 18.7374 |
| 1990's | 3 (75.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Michaud, C; Orlowski, M | 1 |
| Enghild, JJ; Pizzo, SV; Thøgersen, IB; Valnickova, Z | 1 |
| Cardozo, C; Eleuteri, AM; Orlowski, M | 1 |
| Cardozo, C; Michaud, C; Orlowski, M | 1 |
4 other study(ies) available for isocoumarins and alpha-chymotrypsin
| Article | Year |
|---|---|
Pituitary multicatalytic proteinase complex. Specificity of components and aspects of proteolytic activity.
Topics: Amino Acid Sequence; Animals; Cattle; Chymotrypsin; Coumarins; Cysteine Endopeptidases; Endopeptidases; Enzyme Activation; Fatty Acids; Heparin; Immune Sera; Isocoumarins; Molecular Sequence Data; Multienzyme Complexes; Oligopeptides; Phosphorylation; Pituitary Gland; Proteasome Endopeptidase Complex; Proteins; Serine Endopeptidases; Serine Proteinase Inhibitors; Sodium Dodecyl Sulfate; Substrate Specificity; Trypsin | 1989 |
Complexes between serpins and inactive proteinases are not thermodynamically stable but are recognized by serpin receptors.
Topics: alpha-2-Antiplasmin; Amino Acid Sequence; Animals; Chymotrypsin; Coumarins; Endopeptidases; Enzyme Stability; Humans; Isocoumarins; Leukocyte Elastase; Mice; Molecular Sequence Data; Pancreatic Elastase; Protein Conformation; Receptors, Cell Surface; Serpins; Thermodynamics | 1994 |
Differences in catalytic activities and subunit pattern of multicatalytic proteinase complexes (proteasomes) isolated from bovine pituitary, lung, and liver. Changes in LMP7 and the component necessary for expression of the chymotrypsin-like activity.
Topics: Amino Acid Sequence; Animals; Catalysis; Cattle; Chymotrypsin; Coumarins; Cysteine Endopeptidases; Isocoumarins; Liver; Lung; Molecular Sequence Data; Multienzyme Complexes; Pituitary Gland; Proteasome Endopeptidase Complex; Proteins | 1995 |
Evidence for the presence of five distinct proteolytic components in the pituitary multicatalytic proteinase complex. Properties of two components cleaving bonds on the carboxyl side of branched chain and small neutral amino acids.
Topics: Amino Acid Sequence; Animals; Calcium; Cattle; Chymotrypsin; Coumarins; Cysteine Endopeptidases; Isocoumarins; Kinetics; Lauric Acids; Magnesium; Molecular Sequence Data; Multienzyme Complexes; Oligopeptides; Pituitary Gland; Protease Inhibitors; Proteasome Endopeptidase Complex; Serine Proteinase Inhibitors; Sodium Dodecyl Sulfate; Substrate Specificity; Trypsin | 1993 |