Results 311 to 320 of about 665,350 (364)
Specific recognition of mitochondrial preproteins by the cytosolic domain of the import receptor MOM72 [PDF]
, 1994 Dietmeier, Klaus A. +3 more
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Immobilization of Porcine Trypsin in Superparamagnetic Nanoparticles: Enzyme Activity and Stability. [PDF]
ACS OmegaAversa IFS +9 more
europepmc +1 more source
Bioactive Plant Peptides: Physicochemical Features, Structure-Function Insights and Mechanism of Action. [PDF]
MoleculesAvilés-Gaxiola S +4 more
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Biochemical and Biophysical Research Communications, 1982
Abstract The denaturation of α- and β-trypsin in alkaline and neutral solution was studied. The denaturation of α-trypsin was a strict second-order reaction at neutrality. However, the denaturation of β-trypsin was not a pure secondorder reaction at the same pH.
Myron L. Bender +2 more
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Abstract The denaturation of α- and β-trypsin in alkaline and neutral solution was studied. The denaturation of α-trypsin was a strict second-order reaction at neutrality. However, the denaturation of β-trypsin was not a pure secondorder reaction at the same pH.
Myron L. Bender +2 more
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Journal of Allergy, 1964
T rypsin (Parenzyme) is used extensively in the treatment of a variety of disorders.1-26 These conditions include thrombophlebitis, peripheral vascular disease, venous thrombosis, postoperative edema, traumatic swelling, hematomas, ulcerative lesions, postphlebitic syndrome, etc.
Leo H. Criep, Lewis R. Beam
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T rypsin (Parenzyme) is used extensively in the treatment of a variety of disorders.1-26 These conditions include thrombophlebitis, peripheral vascular disease, venous thrombosis, postoperative edema, traumatic swelling, hematomas, ulcerative lesions, postphlebitic syndrome, etc.
Leo H. Criep, Lewis R. Beam
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The Journal of Biochemistry, 1982
We devised a new separation technique for the protein, "affinophoresis," which is based on its specific affinity and utilizes electrophoresis. This technique requires a carrier macromolecule, "affinophore," which contains both an affinity ligand for a certain protein and many charges, either positive or negative, in order to migrate rapidly in an ...
Ken-ichi Kasai, Kiyohito Shimura
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We devised a new separation technique for the protein, "affinophoresis," which is based on its specific affinity and utilizes electrophoresis. This technique requires a carrier macromolecule, "affinophore," which contains both an affinity ligand for a certain protein and many charges, either positive or negative, in order to migrate rapidly in an ...
Ken-ichi Kasai, Kiyohito Shimura
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Journal of Gastroenterology, 2006
Trypsin activity is properly suppressed in the pancreatic acinar cells under normal conditions. A small amount of trypsinogen is converted to active trypsin and inactivated by pancreatic secretory trypsin inhibitor (PSTI), thereby preventing damage to pancreatic acinar cells as a first line of defense.
Masaki Ohmuraya +2 more
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Trypsin activity is properly suppressed in the pancreatic acinar cells under normal conditions. A small amount of trypsinogen is converted to active trypsin and inactivated by pancreatic secretory trypsin inhibitor (PSTI), thereby preventing damage to pancreatic acinar cells as a first line of defense.
Masaki Ohmuraya +2 more
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Journal of Chemical Education, 1977
Adaptation of an experiment entitled "The Turnover Number of Trypsin and Chymotrypsin" to illustrate the difference in basing enzyme concentration on weight, absorbance, or active sites; and that the method chosen to express enzyme concentration determines the calculated value of specific, molecular, and catalytic center activity.
Tom Holzman, Salvatore F. Russo
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Adaptation of an experiment entitled "The Turnover Number of Trypsin and Chymotrypsin" to illustrate the difference in basing enzyme concentration on weight, absorbance, or active sites; and that the method chosen to express enzyme concentration determines the calculated value of specific, molecular, and catalytic center activity.
Tom Holzman, Salvatore F. Russo
openaire +3 more sources
Trypsinogen, Trypsin, Trypsin-Substrate and Trypsin-Inhibitor Complexes in Urea Solutions
European Journal of Biochemistry, 1968The denaturation in urea of trypsinogen, trypsin and trypsin derivatives is first-order with respect to protein. 1 Structural modifications affecting the trypsinogen molecule were detected by studying the influence of pH on the rate of denaturation. The acidification of trypsinogen leads to the appearance of 2 reversible equilibria I′⇌ II′⇌ III′
M. Delaage, M. Lazdunski
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Canadian Journal of Research, 1947
Details are given of a colorimetric method for the estimation of trypsin that can be utilized for the evaluation of the proteolytic activity of pancreatic secretion. Being an adaptation of a method that has been used successfully in a clinical laboratory for many years, it is suitable for routine clinical use.
J. M. Bowman, F. D. White
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Details are given of a colorimetric method for the estimation of trypsin that can be utilized for the evaluation of the proteolytic activity of pancreatic secretion. Being an adaptation of a method that has been used successfully in a clinical laboratory for many years, it is suitable for routine clinical use.
J. M. Bowman, F. D. White
openaire +3 more sources