Results 251 to 260 of about 540,123 (302)

The denaturation of trypsin

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.
H L, Wu, C, Kundrot, M L, Bender
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The denaturation of crustacyanin

Archives of Biochemistry and Biophysics, 1964
Abstract The shell pigments of the lobster have been separated into three fractions, α-crustacyanin, β-crustacyanin, and a yellow pigment, by chromatography on DEAE-cellulose. The prosthetic group of all three pigments is the red carotenoid, astaxanthin.
W P, JENCKS, B, BUTEN
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The denaturation of DNA [PDF]

open access: possibleGene, 1993
Nucleic acids display a very characteristic ultraviolet absorption spectrum with a maximum near 260 nm and a minimum near 230 nm. It was discovered in 1950 that the spectrum of native DNA is much lower than the spectrum calculated from its constituent nucleotides (nt). The observed absorbance strongly increases (hyperchromic effect), not only following
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The denaturation of orosomucoid

Archives of Biochemistry and Biophysics, 1982
Abstract Highly purified human orosomucoid exhibits apparent multistate behavior on thermal denaturation, with Δ H (cal) for the transition being 119 kcal/mol at pH 7.4. Asialoorosomucoid denatured similarly. A domain structure could not be demonstrated for orosomucoid with cyanogen bromide fragments, although some reannealing of these did occur.
H B, Halsall, T L, Kirley
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The denaturation of ribonuclease A by combinations of urea and salt denaturants

Journal of Molecular Biology, 1979
Abstract When urea is added to ribonuclease A that has already been denatured by salt (CaCl2, LiClO4 or LiCl were used), a second co-operative transition occurs, supporting the previous demonstration that these salts cause only partial denaturation. Also we have studied the effect of the salts on the urea denaturation, and the effect of urea on the ...
F, Ahmad, C C, Bigelow
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Denaturation of Fish Proteins

Nature, 1957
REPORTING on the influence of freezing-rate on the denaturation of cold-stored fish, Love1 states that organoleptically determined toughness of cod, stored at − 30° C., does not always involve decreased protein solubility.
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