Studies in the Physical Chemistry of the Proteins. Ii. T~e Relation between the Solubility of Casein and Its Capacity to Combine with Base. the Solubility of Casein in Systems Containing the Protein and Sodium Hydroxide.*
نویسنده
چکیده
"Casein is known to have the character of a weak acid; it reddens wet l i tmus paper and forms salt-like compounds with metals. ''~ Thus Laqueur and Sackur began their classic paper on casein near ly 20 years ago3 Moreover, the relat ive strength of this acid was suggested even before m o d e m methods were available for its determinat ion, since i t "has the power of expelling carbonic anhydride from soluble carbonates and bicarbonates. ''~ The amount of base with which it combines at acid, a t neutral , and at alkaline reactions has perhaps been investigated more often than any similar react ion
منابع مشابه
In Vitro Cytotoxic Activity and Binding Properties of Curcumin in the Presence of β-Casein Micelle Nanoparticles
Curcumin (CUR) is the active curcuminoid with many physiological, biochemical, and pharmacological properties. Solubility and stability of CUR is the limiting factors for realizing its therapeutic potential. Bovine β-casein is an abundant milk protein that is highly amphiphilic and self-assembles into stable micellar nanoparticles in aqueous solution. β-Casein nanoparticle can solubilize CUR mo...
متن کاملThe Effect of Hoffmeister Salts on the Chaperoning Action of β-Casein in Preventing Aggregation of Reduced β-Lactalbumin
Protein aggregation and precipitation is associated with many debilitating diseases including Alzheimer's, Parkinson's, and light-chain amyloidosis. β-Casein, a member of the casein family, has been demonstrated to exhibit chaperone-like activity to protect protein form aggregation. Hofmeister salts (lyotropice series) are a class of ions which have an effect on the solubility and also the stab...
متن کاملThe chaperone ability comparison of norma II-casein and modified d-casein upon interaction with lysozinie
Diminishing protein aggregation by chaperone is very important factor in medicine and industry. In this paper, itis induced the chaperone ability for 0-casein upon modification of its acidic residues by Woodward reagentK(WRK) and examined on lysozyme as a target protein at pH 7.2 and outlined the mechanism for chaperoneability of modified system by UV-Vis and fluorescence spectroscopy and theor...
متن کاملExploring the Interaction Mechanism of Coumarin with Bovine β-Casein: Spectrofluorometric and Molecular Modeling Studies
This paper is designed to examine the binding behavior of Coumarin with bovine -casein (βCN) through fluorescence spectroscopy and molecular modeling techniques. The data analysis on fluorescence titration experiments at various temperatures represents the enthalpy driven nature for the formation of Coumarin–βCN complex and the prevailed role of hydrogen bonds and van der Waals interactions in...
متن کاملInvestigation the protective ability of Pulicaria. undulata aqueous extract on aggregation of κ -casein
Protein aggregation is phenomenon wherein protein loses its native structure and aggregates due to the adaption of non-native conformation. Amyloid aggregation formed by the accumulation of various proteins causes many diseases in humans and other organisms. Antioxidants can prevent proteins aggregation. Pulicaria undulata extract along with phenolic compounds can increase protein stability an...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
دوره شماره
صفحات -
تاریخ انتشار 2003