Results 261 to 270 of about 6,129,258 (331)

Functionalized microcrystalline cellulose crosslinked via diisocyanate-derived urethane bonds for wastewater treatment. [PDF]

open access: yesSci Rep
Lail BA   +9 more
europepmc   +1 more source

Cross-continental soil prokaryotic phenotypic traits driven by precipitation regime and land cover

open access: yes
Donhauser J   +8 more
europepmc   +1 more source

Optimum pH for nuclear sex identification using quinacrine

Clinical Genetics, 1975
Preparations 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
semanticscholar   +3 more sources

Electrochemical consideration on the optimum pH of bilirubin oxidase.

Analytical Biochemistry, 2007
Steady-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
semanticscholar   +3 more sources

The optimum pH of adsorbed ribonuclease.

Biochimica et Biophysica Acta, 1959
L. B. Barnett, H. Bull
semanticscholar   +3 more sources

Zur Frage des pH-Optimums des Pepsins

Experientia, 1961
Natural 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
openaire   +1 more source

Concerning the pH optimum of peptic hydrolysis

Archives of Biochemistry and Biophysics, 1955
Abstract 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.
openaire   +2 more sources

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