alpha-chymotrypsin and 4-maleimido-2-2-6-6-tetramethylpiperidinooxyl

alpha-chymotrypsin has been researched along with 4-maleimido-2-2-6-6-tetramethylpiperidinooxyl* in 2 studies

Other Studies

2 other study(ies) available for alpha-chymotrypsin and 4-maleimido-2-2-6-6-tetramethylpiperidinooxyl

Article	Year
Effect of proteolysis on the electron spin resonance spectra of maleimide spin labeled erythrocyte membrane. Biochimica et biophysica acta, 1985, Dec-05, Volume: 821, Issue:2 The ratio of low-field amplitudes of weakly and strongly immobilized signals of ESR spectra of a maleimide spin label bound to erythrocyte membranes (hw/hs) increases progressively during incubation at 37 degrees C. This increase is due to the 'self-digestion' of membrane proteins by endogenous proteinases and is attenuated by proteinase inhibitors. Digestion of membranes with chymotrypsin also increases the hw/hs ratio. These results suggest a need for a careful interpretation of data from spin-labeled membrane proteins, especially in experiments involving prolonged incubations of membrane preparations when the proteolytic effects may be significant. Topics: Animals; Cattle; Chymotrypsin; Cyclic N-Oxides; Electron Spin Resonance Spectroscopy; Erythrocyte Membrane; Hydrolysis; Membrane Proteins; Protease Inhibitors; Spin Labels; Temperature; Time Factors	1985
Complex formation of guanidinated bovine trypsin inhibitor (Kunitz) with trypsin, chymotrypsin and trypsinogen as studied by the spin-label technique. FEBS letters, 1982, Apr-05, Volume: 140, Issue:1 Topics: Animals; Cattle; Chemical Phenomena; Chemistry; Chymotrypsin; Cyclic N-Oxides; Electron Spin Resonance Spectroscopy; Methylurea Compounds; Spin Labels; Trypsin; Trypsin Inhibitor, Kunitz Soybean; Trypsin Inhibitors; Trypsinogen	1982

Article

Year

Effect of proteolysis on the electron spin resonance spectra of maleimide spin labeled erythrocyte membrane.

Biochimica et biophysica acta, 1985, Dec-05, Volume: 821, Issue:2

The ratio of low-field amplitudes of weakly and strongly immobilized signals of ESR spectra of a maleimide spin label bound to erythrocyte membranes (hw/hs) increases progressively during incubation at 37 degrees C. This increase is due to the 'self-digestion' of membrane proteins by endogenous proteinases and is attenuated by proteinase inhibitors. Digestion of membranes with chymotrypsin also increases the hw/hs ratio. These results suggest a need for a careful interpretation of data from spin-labeled membrane proteins, especially in experiments involving prolonged incubations of membrane preparations when the proteolytic effects may be significant.

Topics: Animals; Cattle; Chymotrypsin; Cyclic N-Oxides; Electron Spin Resonance Spectroscopy; Erythrocyte Membrane; Hydrolysis; Membrane Proteins; Protease Inhibitors; Spin Labels; Temperature; Time Factors

1985

Complex formation of guanidinated bovine trypsin inhibitor (Kunitz) with trypsin, chymotrypsin and trypsinogen as studied by the spin-label technique.

FEBS letters, 1982, Apr-05, Volume: 140, Issue:1

Topics: Animals; Cattle; Chemical Phenomena; Chemistry; Chymotrypsin; Cyclic N-Oxides; Electron Spin Resonance Spectroscopy; Methylurea Compounds; Spin Labels; Trypsin; Trypsin Inhibitor, Kunitz Soybean; Trypsin Inhibitors; Trypsinogen

1982