The present invention provides a protein aggregation inhibitor for use in preventing aggregation of a protein, containing a crosslinked polymer obtained by polymerizing polymerizable polymer components containing a sulfobetaine polymer obtained by polymerizing monomer components containing a sulfobetaine monomer, the sulfobetaine monomer, and a crosslinkable monomer.

Disclosed are methods for isolating polymerase complexes from a mixture of polymerase complex components. The polymerase complexes can comprise a nanopore to provide isolated nanopore sequencing complexes. The methods relate to the positive and negative isolation of the polymerase complexes and/or nanopore sequencing complexes. Also disclosed is a nucleic acid adaptor for isolating active polymerase complexes, polymerase complexes comprising the nucleic acid adaptor, and methods for isolating active polymerase complexes using the nucleic acid adaptor.

Disclosed are methods for isolating polymerase complexes from a mixture of polymerase complex components. The polymerase complexes can comprise a nanopore to provide isolated nanopore sequencing complexes. The methods relate to the positive and negative isolation of the polymerase complexes and/or nanopore sequencing complexes. Also disclosed is a nucleic acid adaptor for isolating active polymerase complexes, polymerase complexes comprising the nucleic acid adaptor, and methods for isolating active polymerase complexes using the nucleic acid adaptor.

By using a mutant glucose oxidase comprising an amino acid sequence in which a residue corresponding to isoleucine at position 489 or arginine at position 335 in the amino acid sequence of SEQ ID NO:1 is substituted with an amino acid residue having a reactive functional group in a side chain, and binding an electron acceptor to the mutant glucose oxidase through the amino acid residue having a reactive functional group, an electron acceptor-modified glucose oxidase is obtained.

By using a mutant glucose oxidase comprising an amino acid sequence in which a residue corresponding to isoleucine at position 489 or arginine at position 335 in the amino acid sequence of SEQ ID NO:1 is substituted with an amino acid residue having a reactive functional group in a side chain, and binding an electron acceptor to the mutant glucose oxidase through the amino acid residue having a reactive functional group, an electron acceptor-modified glucose oxidase is obtained.

A process for providing a mono-PEGylated protein composition is provided. The process is particularly suitable for providing mono-PEGylated erythropoietin composition. The process comprises subjecting a mixture comprising non-PEGylated, mono-PEGylated and oligo-PEGylated to a hydrophobic interaction chromatography process.

A process for providing a mono-PEGylated protein composition is provided. The process is particularly suitable for providing mono-PEGylated erythropoietin composition. The process comprises subjecting a mixture comprising non-PEGylated, mono-PEGylated and oligo-PEGylated to a hydrophobic interaction chromatography process.

Complexes comprising a nucleic acid-guided endonuclease, a sequence-specific targeting nucleic acid and an amphipathic helical peptide are provided. Compositions and methods for delivery of complexes comprising a nucleic acid-guided endonuclease, a sequence-specific targeting nucleic acid and an amphipathic helical peptide to mammals for both research and therapeutic use are provided. Methods of treating or reducing one or more symptoms of type 2 diabetes, prediabetes and/or gestational diabetes are provided.

Complexes comprising a nucleic acid-guided endonuclease, a sequence-specific targeting nucleic acid and an amphipathic helical peptide are provided. Compositions and methods for delivery of complexes comprising a nucleic acid-guided endonuclease, a sequence-specific targeting nucleic acid and an amphipathic helical peptide to mammals for both research and therapeutic use are provided. Methods of treating or reducing one or more symptoms of type 2 diabetes, prediabetes and/or gestational diabetes are provided.

Described herein is a liquid enzyme preparation containing component (a): at least one salt according to general formula (I)
(R.sup.2).sub.3N.sup.+—(CH.sub.2).sub.nC(R.sup.3)(R.sup.4)—(O—X).sub.m—O—C(O)—R.sup.1A.sup.−  (I) wherein n is selected from 1 to 12, m is selected from zero to 50, R.sup.1 is selected from the group consisting of methyl, ethyl, —CH(OH)—CH(OH)—COOH, CH(OH)—CH.sub.3, (E)-CH═CHCOOH, (Z)—CH═CHCOOH, —C.sub.6H.sub.5, para-HO—C.sub.6H.sub.4—, o,p-dihydroxyphenyl, and 3,4,5-triydroxyphenyl, R.sup.2 are same or different and selected from C.sub.1-C.sub.10-alkyl, phenyl, R.sup.3 and R.sup.4 are same or different and selected from hydrogen and C.sub.1-C.sub.4-alkyl, X is C.sub.2-C.sub.4-alkylen, and A.sup.− is an inorganic or organic counteranion,
component (b): at least one enzyme selected from hydrolases (EC 3),
and
optionally component (c): at least one compound selected from enzyme stabilizers different from component (a), preservatives, and surfactants.