Results 271 to 280 of about 99,088 (315)
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A useful spectrophotometric rate assay for pepsin
Analytical Biochemistry, 1971Abstract Phenyl sulfite is a specific substrate for pepsin, whose hydrolysis can be followed spectrophotometrically. This compound is superior to peptide substrates in its ease of synthesis and its ability to be monitered spectrophotometrically. The sulfite assay is therefore the method of choice for both routine and detailed assays of pepsin.
T P, Stein, T W, Reid, D, Fahrney
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Pepsin as a Marker for Pulmonary Aspiration
American Journal of Critical Care, 2002• Background Although assessment for aspiration of small volumes of gastric contents in tube-fed patients receiving mechanical ventilation is important, available methods for this purpose are not wholly satisfactory. A potential method is immunoassay of tracheal secretions for the gastric enzyme pepsin.
Norma A, Metheny +8 more
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Chicken Pepsin as a Rennet Substitute
Canadian Institute of Food Science and Technology Journal, 1984Abstract Semi-purified chicken pepsin was prepared from proventriculae at a yield of 33% of the original pepsin activity using a procedure based on the method described by Bohak (1970) . Cheddar cheese was produced using the chicken pepsin preparation, and with calf rennet as a control, in two trials.
C.J. Findlay, D.W. Stanley, D.B. Emmons
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Pepsin and antacid therapy: A dilemma
Journal of Chemical Education, 1979Illustrates some areas of uncertainty in the current literature regarding the mechanism of digestion and presents an experiment that is more consistent with current biochemical research.
Patty H. Laswick, W. Brayton Batson
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A History Of Pepsin And Related Enzymes
The Quarterly Review of Biology, 2002Studies on gastric digestion during 1820-1840 led to the discovery of pepsin as the agent which, in the presence of stomach acid, causes the dissolution of nutrients such as meat or coagulated egg white. Soon afterward it was shown that these protein nutrients were cleaved by pepsin to diffusible products named peptones.
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Gastrin, a Stimulant of Pepsin Secretion
Archives of Surgery, 1963In theoretical considerations of the mechanism of gastric secretion, suggestions have been made that irrespective of whether the initial stimulus to the gastric glands is nervous by way of the vagi or hormonal by way of gastrin, the ultimate final common pathway for these stimuli may be the release of histamine.
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A turbidimetri milk-clotting assay for pepsin
Analytical Biochemistry, 1976Abstract The action of pepsin on a dilute solution of skim milk produces a sigmoidal increase in the turbidity of the solution. The time course of the increase depends on the amount of pepsin present. Turbidity changes can be measured in a recording spectrophotometer, providing an automated form of the milk clotting assay, which will easily determine
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The Journal of Biochemistry, 1980
The fluorescence of pepsin-bound 2-p-toluidinylnaphthalene-6-sulfonate (TNS) decreases upon the binding of Streptomyces pepsin inhibitor (SPI) with the enzyme. Equilibrium dialysis experiments showed this decrease to arise from the release of TNS from pepsin due to the binding of SPI in a molar ratio of 1 : 1.
K, Kitagishi, H, Nakatani, K, Hiromi
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The fluorescence of pepsin-bound 2-p-toluidinylnaphthalene-6-sulfonate (TNS) decreases upon the binding of Streptomyces pepsin inhibitor (SPI) with the enzyme. Equilibrium dialysis experiments showed this decrease to arise from the release of TNS from pepsin due to the binding of SPI in a molar ratio of 1 : 1.
K, Kitagishi, H, Nakatani, K, Hiromi
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V. A Delayed Effect of X Rays on Pepsin
The British Journal of Radiology, 1954The inactivation of pepsin by X rays consists of two separable parts, an immediate inactivation and a slowly developing one having a high temperature coefficient of inactivation. The slow reaction is quantitatively larger than the initial one. The slow reaction depends on some modification of the protein during the irradiation.
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1995
Proteins are normally analysed by Electrospray Mass Spectrometry (ESMS) as their multiply charged positive ions, when their molecular masses are typically measured to within 0.01% of the values calculated from the primary sequences. The aspartic proteinases obtained from gastric secretions, however, have an insufficient number of basic amino acids to ...
Green, B. N. +3 more
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Proteins are normally analysed by Electrospray Mass Spectrometry (ESMS) as their multiply charged positive ions, when their molecular masses are typically measured to within 0.01% of the values calculated from the primary sequences. The aspartic proteinases obtained from gastric secretions, however, have an insufficient number of basic amino acids to ...
Green, B. N. +3 more
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