Kinetic analysis of soy-protein denaturation by a temperature-programmed heat-denaturation technique.
نویسندگان
چکیده
منابع مشابه
Mechanical denaturation of DNA: existence of a low temperature denaturation
Recent theoretical predictions on DNA mechanical separation induced by pulling forces are numerically tested within a model in which self-avoidance for DNA strands is fully taken into account. DNA strands are described by interacting pairs of self avoiding walks (SAW) which are pulled apart by a force applied at the two extremities. The whole phase diagram is spanned by extensive Monte Carlo (M...
متن کاملPressure and protein denaturation.
Kinetic analyses have indicated that moderate hydrostatic pressures, up to some 700 atmospheres, oppose reversible and irreversible denaturations of certain enzyme systems, apparent at temperatures above the normal optimum of the enzyme reaction, as well as at lower temperatures in the presence of denaturants such as alcohol (14). Qualitative observations have shown that such pressures also ret...
متن کاملHeat shock responses for understanding diseases of protein denaturation.
Extracellular stresses induce heat shock response and render cells resistant to lethal stresses. Heat shock response involves induction of heat shock proteins (Hsps). Recently the roles of Hsps in neurodegenerative diseases and cancer are attracting increasing attention and have accelerated the study of heat shock response mechanism. This review focuses on the stress sensing steps, molecules in...
متن کاملNature of Heat Denaturation of Proteins
Chick and Martin (1) have shown that the heat coagulation of proteins consists of two distinct processes; tiiz., (a) denaturation, the alteration of the protein under the influence of heat, and (b) agglutination, the separation of the altered protein in a particulate form. Agglutination, in which hydrogen ion concentration and electrolyte contents play important roles (2), is now a fairly well ...
متن کاملThe Reversible Heat Denaturation of Chymotrypsinogen
Within a restricted range of pH and protein concentration crystalline chymotrypsinogen undergoes thermal denaturation which is wholly reversed upon cooling. At a given temperature an equilibrium exists between native and reversibly denatured protein. Within the pH range 2 to 3 the amount of denatured protein is a function of the third power of the hydrogen ion activity. The presence of small am...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1990
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.54.863