Results 271 to 280 of about 50,025 (309)
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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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Determination of chymosin and bovine pepsin A in commercial bovine rennets and pepsins
1981International ...
Collin, J.C. +4 more
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A pepsin preparation without transpeptidation activity
Biochimica et Biophysica Acta, 1960H, NEUMANN, N, SHARON
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The Journal of Peptide Research, 1999
Abstract: Porcine pepsin in water solutions containing 15–28% of dimethylformamide at pH 5 and 20–37°C catalysed the formation of peptide bonds between Z‐Ala‐Ala‐Phe‐OH and various amino acid or peptide derivatives. Substrate binding subsite S′1 of pepsin demonstrated broad specificity in these reactions but revealed a certain preference for ...
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Abstract: Porcine pepsin in water solutions containing 15–28% of dimethylformamide at pH 5 and 20–37°C catalysed the formation of peptide bonds between Z‐Ala‐Ala‐Phe‐OH and various amino acid or peptide derivatives. Substrate binding subsite S′1 of pepsin demonstrated broad specificity in these reactions but revealed a certain preference for ...
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A study of the individual peptides of a pepsin hydrolyzate of pepsin
Chemistry of Natural Compounds, 1972V. I. Vasenev +2 more
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