The invention provides methods and systems for production of recombinant protein, and particularly, for production of recombinant protein from inclusion bodies. For example, in one aspect, the method comprises providing a protein preparation comprising inclusion bodies, preparing an inclusion body dispersion, and exposing the protein preparation to high pressure in a pressure vessel, to disaggregate and refold the inclusion body protein.

The present invention provides method of increasing the percentage of monomer in a composition of recombinantly expressed antibody molecules characterised in that the antibody molecule comprises at least one Fv with specificity for an antigen of interest comprising one VH and one VL wherein said VH and VL are connected directly or indirectly via one or more linkers and are stabilised by a disulfide bond therebetween, said method comprises: a) a conversion step of treating the composition with a denaturant selected from urea and/or Guanidine hydrochloride; b) wherein step a) is performed in the presence of a reducing agent or after treatment with a reducing agent.

One subject of the present invention is the use of a combination of a polyol (i) consisting of 12 carbon atoms and of a polyol (ii) consisting of 4 to 6 carbon atoms, as protein stabilizer. Another subject of the present invention is protein compositions comprising such a combination. A final subject of the present invention is a process for preparing protein compositions using such a combination.

Disclosed is a method for refolding a protein or peptide that does not contain essential disulfides and that contains at least one free cysteine residue. Also disclosed are polymer IFN- conjugates that have been created by the chemical coupling of polymers such as polyethylene glycol moieties to IFN-, particularly via a free cysteine in the protein. Also disclosed are analogs of bioactive peptides that may be used to create longer acting versions of the peptides, including analogs of glucagon, glucagon-like peptide-1 (GLP-1), GLP-2, Gastric inhibitory peptide (GIP), PYY, exendin, ghrelin, gastrin, amylin, and oxyntomodulin.

This application describes a compound represented by Formula (I):
YZX.sup.1S(O)(X.sup.2)F).sub.m].sub.n(I)
wherein: Y is a biologically active organic core group comprising one or more of an aryl group, a heteroaryl aryl group, a nonaromatic hydrocarbyl group, and a nonaromatic heterocyclic group, to which Z is covalently bonded; n is 1, 2, 3, 4 or 5; m is 1 or 2; Z is O, NR, or N; X.sup.1 is a covalent bond or CH.sub.2CH.sub.2, X.sup.2 is O or NR; and R comprises H or a substituted or unsubstituted group selected from an aryl group, a heteroaryl aryl group, a nonaromatic hydrocarbyl group, and a nonaromatic heterocyclic group. Methods of preparing the compounds, methods of using the compounds, and pharmaceutical compositions comprising the compounds are described as well.

A high-throughput screening methods for identifying candidate anticancer medicinal agents is described herein. The candidate anticancer medicinal agents are arylfluorosulfate compounds derived from phenolic compounds. The method involves in situ generation of the arylfluorosulfate compounds in multi-well plates by reaction of phenolic compounds in DMSO with a saturated solution of SO.sub.2F.sub.2 dissolved in a solvent such as acetonitrile, in the presence of an organic base, followed by reaction of generated fluoride ion with trimethylsilyl chloride to form volatile trimethylsilyl fluoride. Solvents, organic base, and silyl compounds are then removed, in vacuo, to afford the arylfluorosulfate compounds suitable for biological screening in cancer cell lines without further purification.

Provided is a method of treating a protein to be renatured, including: (1) mixing the protein to be renatured with a denaturing solution containing a denaturing reagent; (2) incubating a resulting mixture at such a low temperature that the denaturing agent is gradually precipitated from the denaturing solution, resulting in a decreasing concentration gradient of the denaturing agent and an increasing concentration of a renatured protein or its precursor in the denaturing solution with a decreasing volume; and (3) obtaining at least one of the renatured protein and its precursor.

A fiber-treating agent including a condensate formed from the following components (A) and (B), and a component (C). A total content of a constituent element derived from the component (A) and a constituent element derived from the component (B) is more than 1 mass %, and a turbidity is 1,000 NTU or less: (A): formaldehyde or a hydrate thereof, (B): triazine or a derivative thereof of formula (1):

##STR00001## where R.sup.1 to R.sup.3 are the same or different, and each represent a hydrogen atom, a hydroxymethylamino group, an amino group, a hydroxy group, a halogen atom, a phenyl group, a linear or branched alkyl group or alkenyl group having 1 or more and 6 or less carbon atoms, or a linear or branched alkoxy group or alkenyloxy group having 1 or more and 6 or less carbon atoms, and (C): water.

The invention includes a thioamide-modified peptide, wherein the thioamide modification increases the in vivo half-life of the peptide. The invention further includes methods of treating or preventing a disease or disorder in a subject in need thereof, the method comprising administering to the subject a thioamide-modified peptide of the invention.

Processes and apparatuses for producing biologically-active, protein-rich microparticles under ambient conditions are disclosed. A protein solution is atomized and collected in a dehydration solvent that is being mixed. The resulting protein microparticles retain high specific activity without the need for large amounts of stabilizing excipients.