Results 261 to 270 of about 1,963,376 (294)

Immunochemical studies on thermal denaturation of ovomucoid

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
The thermal denaturation of ovomucoid was investigated by immunochemical methods, namely immunoprecipitation analyses and antibody-Sepharose 4B column chromatography. In the immunoprecipitation analyses, heated ovomucoid (90 degrees C, 90 min, pH 7.2) required about twice the antigen addition of the native protein to approach maximal precipitation with
T, Matsuda, K, Watanabe, R, Nakamura
openaire   +2 more sources

Effects of thermal denaturation on protein glycation

Life Sciences, 2002
Protein 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
openaire   +2 more sources

Ligand-induced biphasic thermal denaturation of RNAase A

Journal of Thermal Analysis, 1994
DSC measurements have been accomplished in aqueous solutions of bovine pancreatic ribonuclease A (RNAase A) in the presence of subsaturating amounts of 3′ cytidine monophosphate (3′ CMP) and 2′ cytidine monophosphate (2′ CMP) atpH 5.0 and 5.5. In these conditions the experimental profiles do not conform to a one-step unfolding process.
G. BARONE, DEL VECCHIO, POMPEA GIUSEPPINA GRAZIA, D. FESSAS, GIANCOLA, CONCETTA, G. GRAZIANO, A. RICCIO   +5 more
openaire   +5 more sources

A SIMPLE MODEL FOR PROTEIN THERMAL DENATURATION*

International Journal of Peptide and Protein Research, 1978
Whether 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.
openaire   +2 more sources

Thermal denaturation profiles and the structure of chromatin

Nature, 1976
Analysis of the melting profile of DNA stripped of non-histone proteins and histone H1 allows definite structural conclusions to be drawn; conversely, it is possible to calculate what a particular chromatin model's melting curve will look like.
openaire   +2 more sources

Denaturation kinetics of biopolymers by differential thermal analysis

Journal of the American Chemical Society, 1967
SEVERAL workers have described equations to calculate the activation energy of a reaction from the exothermic or endothermic peaks which occur during a differential thermal analysis (DTA) experiment1–3. There is a second type of differential thermal analysis curve, one not characterized by a maximum or a minimum but by a sigmoid shape caused by a ...
openaire   +2 more sources

On the thermal denaturation of glucose oxidase

Biotechnology and Bioengineering, 1982
C O, Malikkides, R H, Weiland
openaire   +2 more sources

Thermal denaturation of DNP

Bulletin of Experimental Biology and Medicine, 1973
N. V. Chelyapov, A. I. Gorin, V. N. Sudarev, P. I. Tseitlin   +3 more
openaire   +1 more source

Thermal denaturation of ribosomes

Biochemistry, 1969
openaire   +2 more sources

Thermal denaturation of alpha-crystallin.

Lens and eye toxicity research, 1991
Low 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
openaire   +1 more source