Isoelectric points of proteins, determined by isoelectric focusing in the presence of urea and ethanol

Isoelectric focusing.

Isoelectric points of multi-domain proteins

Although the distribution of protein isoelectric points is multi-modal, large proteins show isoelectric points less variable than small proteins and their isoelectric points tend to converge to a unique value, close to the pH of the milieu in which the proteins are functional, as far as the protein dimension increases. This study demonstrates that large proteins, which contain more than a singl...

Antigenic characterization of flavivirus structural proteins separated by isoelectric focusing.

Isoelectrofocusing of nonionic-detergent-disrupted flaviviruses separated the envelope glycoprotein of 53,000 to 58,000 daltons and the nucleocapsid protein of 14,000 daltons. The envelope protein and nucleocapsid protein were isolated at isoelectric points of pI 7.8 and 10.3, respectively. The antigenic determinants of St. Louis encephalitis, Japanese encephalitis, and dengue virus envelope an...

Isoelectric points of viruses.

Viruses as well as other (bio-)colloids possess a pH-dependent surface charge in polar media such as water. This electrostatic charge determines the mobility of the soft particle in an electric field and thus governs its colloidal behaviour which plays a major role in virus sorption processes. The pH value at which the net surface charge switches its sign is referred to as the isoelectric point...

The Isoelectric Points of the Proteins in Certain Vegetable Juices

The state in which a protein substance exists depends upon the nature of its combination with acids or bases and is changed by change in the protein compound. The nature of the compound of a protein that exists at any hydrogen ion concentration can be ascertained if the isoelectric point of the protein is known. Accordingly information regarding the isoelectric points of vegetable proteins is o...