C07K1/303

High Efficiency Methods for Isolating Proteins

Systems and methods are described in which proteins are isolated from complex solutions in high yield and at high purity. Such systems and methods are carried out at ambient temperature and can be carried out at industrial scale with minimal energy requirements and minimal carbon footprint, using successive chromatographic separations that retain the protein or proteins of interest in flow-through fractions. At least one of the chromatography media used is selected to be capable of interacting with both contaminants and the protein of interest, however capacity of this media is selected such that the protein of interest is displaced and remains in the flow-through. Methods for isolation of IgG, albumin, and both IgG and albumin are provided.

USE OF A TETRAPHENYLBORATE (TPB) SALT FOR THE SEPARATION OF BIOMOLECULES
20170183375 · 2017-06-29 ·

Process for the separation of a biomolecule containing at least one cationic group from a liquid medium containing said biomolecule, which comprises the use of a tetraphenylborate (TPB) salt.

PRECIPITABLE PEPTIDES

The invention is directed to a Ca2+ precipitable polypeptide tags and cassettes useful for purification of molecules from heterogeneous samples. The invention also relates to methods for bioseparation of molecules comprising Ca2+ precipitable tags and cassettes.

Real time monitoring and control of protein production processes using impedance spectroscopy

Methods and systems for monitoring and/or controlling protein separation, purification, extraction, and/or fractionation processes are provided. The impedance of a protein mixture undergoing a protein process is measured and compared to a target reference impedance value or range of reference impedance values. If the measured impedance is not within an acceptable deviation of the target reference impedance value, a parameter of the protein mixture or process is adjusted.

Plasma protein fractionation by sequential polyacid precipitation

There is a recognized need for novel, more simplified, approaches to isolation of plasma from whole blood, as well as a need to isolate cell-free plasma fractions containing different plasma proteins. Methods are divulged for use of aqueous phase systems, formed in blood or blood containing solutions via addition of a single polymer at relatively low concentration, to effect isolation (clarification) of plasma proteins from blood cells. Methods are also divulged to replace widely used Cohn-type plasma protein fractionation which is based on sequential addition of up to 40% (v/v) ethanol and other precipitants, with simple sequential addition of a polyacid. The latter results in isolation of plasma protein fractions (i.e. fibrinogen, immunoglobulin, albumin) in sequence similar to that obtained with Cohn Fractionation and therefore may be suitable for use to reduce solvent use and solvent-related process complications in existing plasma protein purification processes. It may also support use of polymeric film based containers in novel solvent free plasma fractionation processes. The methods disclosed may also be suitable for use in smaller scale plasma protein isolation, in research and diagnostic applications. The general methodologies are robust and can function over a broad range of process variables such as temperature and pH.

Use of a tetraphenylborate (TPB) salt for the separation of biomolecules

Process for the separation of a biomolecule containing at least one cationic group from a liquid medium containing said biomolecule, which comprises the use of a tetraphenylborate (TPB) salt.

Method for extracting IgY (γ-livetin) from egg yolk

A method for extracting IgY (-livetin) from yolk is disclosed, which comprises the following steps: (A) providing a buffer solution, a yolk sample, and an inorganic salt solution; (B) diluting the yolk sample with the buffer solution to obtain a mixture, stirring the mixture for a predetermined time, and performing a centrifugation on the mixture to obtain a supernatant; and (C) adding the inorganic salt solution into the supernatant to salt out IgY, wherein a pH value of the buffer solution is in a range from 4.6 to 5.4, a salt concentration of the buffer solution is in a range from 0.05 M to 0.15 M, and a saturation degree of the inorganic salt solution is in a range from 30% to 60%.

FRACTIONATION METHOD
20170057992 · 2017-03-02 ·

Provided herein is a novel method of purifying an IgG antibody from a preparation by use of an electropositive membrane having a defined porosity.

Precipitable peptides

The invention is directed to a Ca2+ precipitable polypeptide tags and cassettes useful for purification of molecules from heterogeneous samples. The invention also relates to methods for bioseparation of molecules comprising Ca2+ precipitable tags and cassettes.

METHOD OF PRODUCING COLLAGEN

The present disclosure relates to a method of producing collagen from an animal and more particularly, the present invention relates to a method for producing collagen by applying an acid and metal fluoride combination to an animal skin.