urea and trypsinogen

urea has been researched along with trypsinogen in 16 studies

Research

Studies (16)

TimeframeStudies, this research(%)All Research%
pre-199014 (87.50)18.7374
1990's1 (6.25)18.2507
2000's1 (6.25)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Ishii, S; Kasai, K1
al-Obeidi, AM; Light, A1
Morgan, PH; Neurath, H; Walsh, KA1
Chen, RF1
Knights, RJ; Light, A1
Neurath, H; Reeck, GR1
McNeill, DA; Pond, WG; Snook, JT; Snyder, W; Stillings, BR; Walker, EF1
Herskovits, TT; Villanueva, GB1
Hopkins, TR; Spikes, JD1
Delaage, M; Lazdunski, M1
Neurath, H; Radhakrishnan, TM; Russo, SF; Walsh, KA1
Abita, JP; Lazdunski, M1
Mosolov, VV1
Martins, NF; Santoro, MM1
Xu, Y; Zhou, HM; Zhou, HW1
DREYER, WJ; NEURATH, H; RUPLEY, JA1

Other Studies

16 other study(ies) available for urea and trypsinogen

ArticleYear
Affinity chromatography of trypsin and related enzymes. I. Preparation and characteristics of an affinity adsorbent containing tryptic peptides from protamine as ligands.
    Journal of biochemistry, 1975, Volume: 78, Issue:4

    Topics: Amino Acids; Benzamidines; Chromatography, Affinity; Chymotrypsin; Hydrogen-Ion Concentration; Ligands; Oligopeptides; Osmolar Concentration; Protamines; Sepharose; Streptomyces griseus; Temperature; Trypsin; Trypsinogen; Urea

1975
Size-exclusion high performance liquid chromatography of native trypsinogen, the denatured protein, and partially refolded molecules. Further evidence that non-native disulfide bonds are dominant in refolding the completely reduced protein.
    The Journal of biological chemistry, 1988, Jun-25, Volume: 263, Issue:18

    Topics: Chromatography, High Pressure Liquid; Protein Conformation; Protein Denaturation; Trypsinogen; Urea

1988
Inactivation of trypsinogen by methane sulfonyl fluoride.
    FEBS letters, 1974, Apr-15, Volume: 41, Issue:1

    Topics: Animals; Aspergillus; Binding Sites; Calcium; Cattle; Dimethylformamide; Fluorides; Hydrogen-Ion Concentration; Kinetics; Mesylates; Peptide Hydrolases; Protein Binding; Trypsin; Trypsinogen; Urea

1974
Quenching of the fluorescence of proteins by silver nitrate.
    Archives of biochemistry and biophysics, 1973, Volume: 158, Issue:2

    Topics: Alcohol Oxidoreductases; Binding Sites; Cysteine; Fluorescence; Hydrogen-Ion Concentration; Liver; Mathematics; Osmolar Concentration; Ovalbumin; Protein Binding; Proteins; Saccharomyces cerevisiae; Silver Nitrate; Species Specificity; Spectrometry, Fluorescence; Spectrophotometry; Spectrophotometry, Ultraviolet; Sulfhydryl Compounds; Time Factors; Trypsinogen; Tryptophan; Urea

1973
Sepharose-bound trypsin and activated sepharose-bound trypsinogen. Studies with small and large substrates.
    Archives of biochemistry and biophysics, 1974, Volume: 160, Issue:2

    Topics: Binding Sites; Chromatography, Ion Exchange; Chymotrypsinogen; Cyanogen Bromide; Enzyme Activation; Hydrogen-Ion Concentration; Kinetics; Mathematics; Plants; Polysaccharides; Potentiometry; Protein Binding; Solubility; Spectrophotometry, Ultraviolet; Structure-Activity Relationship; Temperature; Trypsin; Trypsin Inhibitors; Trypsinogen; Urea

1974
Pancreatic trypsinogen from the African lungfish.
    Biochemistry, 1972, Feb-15, Volume: 11, Issue:4

    Topics: Amino Acid Sequence; Amino Acids; Animals; Biological Evolution; Calcium Chloride; Chromatography, DEAE-Cellulose; Chromatography, Gel; Detergents; Electrophoresis, Disc; Electrophoresis, Paper; Enzyme Activation; Fishes; Kinetics; Pancreas; Peptides; Sulfuric Acids; Trypsinogen; Ultracentrifugation; Urea

1972
Relative utilization of casein, fish protein concentrate and isolated soybean protein for growth and pancreatic enzyme regeneration of the protein-calorie malnourished baby pig.
    The Journal of nutrition, 1971, Volume: 101, Issue:9

    Topics: Amino Acids; Amylases; Animal Nutritional Physiological Phenomena; Animals; Blood Glucose; Blood Proteins; Body Weight; Caseins; Cholesterol; Chymotrypsinogen; Deficiency Diseases; Dietary Proteins; Fish Products; Glycine max; Growth; Hemoglobins; Lipase; Pancreas; Plant Proteins; Protein Deficiency; Serum Albumin; Swine; Trypsinogen; Urea

1971
Exposure of the tyrosyl and tryptophyl residues in trypsin and trypsinogen.
    Biochemistry, 1971, Aug-31, Volume: 10, Issue:18

    Topics: Animals; Arginine; Benzyl Compounds; Binding Sites; Calcium Chloride; Catalysis; Cattle; Chemical Phenomena; Chemistry; Chromatography, Ion Exchange; Circular Dichroism; Dimethyl Sulfoxide; Formates; Glucose; Glycerol; Glycols; Hydrogen-Ion Concentration; Lysine; Mathematics; Nitrophenols; Optical Rotatory Dispersion; Protein Conformation; Protein Denaturation; Solvents; Spectrophotometry; Sucrose; Sulfonic Acids; Toluene; Trypsin; Trypsinogen; Tryptophan; Tyrosine; Ultraviolet Rays; Urea

1971
Denaturation of proteins in 8M urea as monitored by tryptophan fluorescence: trypsin, trypsinogen and some derivatives.
    Biochemical and biophysical research communications, 1968, Mar-12, Volume: 30, Issue:5

    Topics: Fluorescence; Fluorometry; Hydrogen-Ion Concentration; Isoflurophate; Protein Denaturation; Trypsin; Trypsinogen; Tryptophan; Urea

1968
Trypsinogen, trypsin, trypsin-substrate and trypsin-inhibitor complexes in urea solutions.
    European journal of biochemistry, 1968, Volume: 4, Issue:3

    Topics: Amidines; Animals; Arginine; Binding Sites; Cattle; Chemical Phenomena; Chemistry, Physical; Drug Stability; Hydrogen-Ion Concentration; Kinetics; Protein Denaturation; Solutions; Trypsin; Trypsin Inhibitors; Trypsinogen; Urea

1968
The inhibition of trypsinogen activation by low concentrations of urea.
    Archives of biochemistry and biophysics, 1969, Volume: 130, Issue:1

    Topics: Amino Acids; Calcium; Fluorometry; Kinetics; Optical Rotatory Dispersion; Peptide Hydrolases; Trypsin Inhibitors; Trypsinogen; Urea

1969
On the structural and functional role of carboxylates in chymotrypsinogen A: a comparison with chymotrypsin, trypsinogen and trypsin.
    Biochemical and biophysical research communications, 1969, Jun-06, Volume: 35, Issue:5

    Topics: Binding Sites; Chemical Phenomena; Chemistry; Chymotrypsin; Drug Stability; Enzyme Precursors; Kinetics; Optical Rotatory Dispersion; Protein Denaturation; Trypsin; Trypsinogen; Urea

1969
[Changes in the conformation of alpha-chymotrypsin and chymotrypsinogen A in the presence of caprinate].
    Doklady Akademii nauk SSSR, 1965, Dec-11, Volume: 165, Issue:5

    Topics: Caproates; Chymotrypsin; Solutions; Trypsinogen; Urea

1965
Partially folded intermediates during trypsinogen denaturation.
    Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas, 1999, Volume: 32, Issue:6

    Topics: Animals; Cattle; Diuretics, Osmotic; Guanidine; Parasympathomimetics; Protein Denaturation; Protein Folding; Trypsinogen; Urea

1999
Activity and conformational changes of horseradish peroxidase in trifluoroethanol.
    Biochemistry and cell biology = Biochimie et biologie cellulaire, 2002, Volume: 80, Issue:2

    Topics: Binding Sites; Circular Dichroism; Electrophoresis, Polyacrylamide Gel; Guanidine; Horseradish Peroxidase; Hydrogen Bonding; Kinetics; Protein Conformation; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Proteins; Spectrometry, Fluorescence; Trifluoroethanol; Trypsinogen; Urea

2002
Structural changes in the activation of chymotrypsinogen and trypsinogen; effect of urea on chymotrypsinogen and delta-chymotrypsin.
    Archives of biochemistry and biophysics, 1956, Volume: 65, Issue:1

    Topics: Chymotrypsin; Chymotrypsinogen; Enzyme Precursors; Hydrolases; Peptide Hydrolases; Trypsin; Trypsinogen; Urea

1956