Results 261 to 270 of about 196,670 (297)
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Kinetics of thermal denaturation of antithrombin III
Biotechnology and Bioengineering, 1982AbstractPurified antithrombin III (AT III), a single‐chain human plasma glycoprotein, molecular weight 58,000 daltons, and one of the major serine protease inhibitors, was heated in the 60–70°C range for inactivating possible contaminations by hepatitis B virus (HBV).
G, Mitra, P M, Schneider, J L, Lundblad
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Dissociative mechanism of F-actin thermal denaturation
Biochemistry (Moscow), 2006We have applied differential scanning calorimetry to investigate thermal unfolding of F-actin. It has been shown that the thermal stability of F-actin strongly depends on ADP concentration. The transition temperature, T(m), increases with increasing ADP concentration up to 1 mM.
V V, Mikhailova +3 more
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Effects of thermal denaturation on protein glycation
Life Sciences, 2002Protein denaturation occurs at sites of inflammation. We hypothesized that denatured protein may provide a more susceptible target for glycation, which is a known mediator of inflammation. We examined the effects of thermal denaturation on the susceptibility of protein glycation using glyceraldehyde 3-phosphate dehydrogenase (GAPDH) and aspartate ...
Norbert W, Seidler, George S, Yeargans
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Thymus deoxyribonucleoprotein I. Preparation and thermal denaturation
Biochimica et Biophysica Acta, 1962Abstract Preparations of undissociated deoxyribonucleoprotein having a reproducible composition were obtained from calf-thymus glands essentially by extraction with water. Spectrophotometric titration and other ultraviolet-absorption measurements showed that this deoxyribonucleoprotein was denatured by heat and by alkali in both 0.001 M and 1.0 M
K, MURRAY, A R, PEACOCKE
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The thermal denaturation of chromatin core particles
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1984The thermal denaturation of chicken erythrocyte core particles has been followed using changes in absorption and circular dichroism. The absorption-denaturation curve is biphasic, with transitions centred at 59 degrees C and 74 degrees C. The first of these transitions is reversible, whereas heating into the second transition produces irreversible ...
I O, Walker, A P, Wolffe
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A SIMPLE MODEL FOR PROTEIN THERMAL DENATURATION*
International Journal of Peptide and Protein Research, 1978Whether proteins denature in an all‐or‐none fashion or in a continuous fashion is as yet an unresolved problem. The all‐or‐none process implies that while the process of denaturation is going on, only two kinds of protein molecules can exist. One is completely unchanged and the other is altered.
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Thermal denaturation of alpha-crystallin.
Lens and eye toxicity research, 1991Low molecular weight alpha-crystallin, isolated from cow lenses, exhibit irreversible thermal denaturation in solution at 75 degrees C. The heat of denaturation was obtained from a differential scanning calorimetric endothermic peak. A second run on the denatured alpha-crystallin solution showed that the denaturation is irreversible.
J A, Castoro, F A, Bettelheim
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Studies on the thermal denaturation of nucleohistones
Journal of Molecular Biology, 1973Abstract The thermal denaturation profiles of nucleohistone from calf thymus, sea urchin sperm and sea cucumber male gonad, are studied and compared under a variety of conditions. These include melting in the presence of either one of the following agents: urea, methanol, divalent cations or excess histones.
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