Functionalized microcrystalline cellulose crosslinked via diisocyanate-derived urethane bonds for wastewater treatment. [PDF]
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Cross-continental soil prokaryotic phenotypic traits driven by precipitation regime and land cover
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Dynamic Modelling of <i>Listeria monocytogenes</i> Growth in a Milk Model Medium as Affected by pH and Selected Lactic Acid Bacteria Strains. [PDF]
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Molecular Interactions of Norfloxacin in Metal-Loaded Clay Suspensions-Effects on Degradation and Induced Toxicity. [PDF]
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Optimum pH for nuclear sex identification using quinacrine
Clinical Genetics, 1975Preparations of quinacrine stained interphase nuclei from buccal smears and hair root sheaths were mounted in Macllvaine's buffer at various pH's in an attempt to obtain optimum differentiation of X‐ and Y‐chromatin. Relatively high pH (5–8) was associated with intense nuclear fluorescence. Background nuclear fluorescence decreased with lower pH's (2–4)
B. Korf, B. Schuh, M. Salwen
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Electrochemical consideration on the optimum pH of bilirubin oxidase.
Analytical Biochemistry, 2007Steady-state current-potential curves were obtained for the direct electron transfer (DET) of bilirubin oxidase (BOD) at a highly oriented pyrolytic graphite electrode, and the theoretical analysis based on nonlinear regression enabled us to determine the formal redox potential (E degrees') of BOD in a wide pH range of 2.0 to 8.5.
Kaori Otsuka +4 more
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The optimum pH of adsorbed ribonuclease.
Biochimica et Biophysica Acta, 1959L. B. Barnett, H. Bull
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Zur Frage des pH-Optimums des Pepsins
Experientia, 1961Natural and purified proteins were split by crystallized pepsin. The break down of substrates was followed by a turbidimetric method. pH optima were found from 1.5 to 3.8. Only unpurified egg albumin had two optima, crystallin had one in the acid range. Ovomucoid not being split by pepsin, the second peak at pH 3.79 is referred to conalbumin. While the
S. Buchs, E. Freudenberg
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Concerning the pH optimum of peptic hydrolysis
Archives of Biochemistry and Biophysics, 1955Abstract The significance of hydrogen-ion concentration to peptic hydrolysis of a number of proteins has been studied in order to throw light upon certain aspects of the activity vs. pH curves. Various denatured substrates are readily hydrolyzed within a wide pH interval.
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