منابع مشابه
Self-assembly of β-casein and lysozyme
The self-assembly of β-casein and lysozyme, a linear and a globular protein with isoelectric point of pH 5.0 and 10.7, respectively, was studied. Polydisperse electrostatic complex micelles formed when mixing β-casein and lysozyme aqueous solutions. After the micelle solution was heated, lysozyme gelated and β-casein was trapped in the gel, producing narrowly dispersed nanoparticles. The nanopa...
متن کاملDetecting β-Casein Variation in Bovine Milk.
In bovine species, β-casein (β-CN) is characterized by genetic polymorphism. The two most common protein variants are β-CN A² (the original one) and A¹, differing from A² for one amino acid substitution (Pro67 to His67). Several bioactive peptides affecting milk nutritional properties can originate from β-CN. Among them, β-casomorphin-7 (BCM7) ranging from amino acid 60 to 66 can be released mo...
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 کاملCloning and Molecular Characterization of Porcine β-casein Gene (CNS2)
The production of therapeutic proteins from transgenic animals is one of the most important successes of animal biotechnology. Milk is presently the most mature system for production of therapeutic proteins from a transgenic animal. Specifically, β-casein is a major component of cow, goat and sheep milk, and its promoter has been used to regulate the expression of transgenic genes in the mammar...
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 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: Journal of the agricultural chemical society of Japan
سال: 1937
ISSN: 0002-1407,1883-6844
DOI: 10.1271/nogeikagaku1924.13.791