A therapeutic agent comprising Lon protease, or a variant or active fragment thereof, alpha-hemolysin, or a variant or active fragment thereof, CK1α1, or a variant or active fragment thereof, a c-MYB inhibitor and/or a CEBP-δ inhibitor, for use in therapy, with the proviso that the therapeutic agent does not comprise a bacteria or bacterial supernatant. Methods of production and use thereof.

It is necessary to establish a purification method effective for the removal of endotoxin, in order to obtain thermolysin containing a reduced amount of contaminant endotoxin. On the premise of the establishment, accurate measurement of the amount of endotoxin that contaminates thermolysin is required. The present invention addresses the problem of providing a novel measurement method which enables accurate measurement of the amount of endotoxin that contaminates thermolysin. The present invention also addresses the problem of providing thermolysin containing a reduced amount of contaminant thermolysin, and the use thereof. There is provided thermolysin containing contaminant endotoxin in an amount of 1 EU/mg or less. There is also provided a method for measuring endotoxin that contaminates thermolysin, the method including pretreatment of deactivating the thermolysin. An enzyme preparation including the thermolysin according to the present invention as an active ingredient has a high utility value in the field of regenerative medicine.

It is necessary to establish a purification method effective for the removal of endotoxin, in order to obtain thermolysin containing a reduced amount of contaminant endotoxin. On the premise of the establishment, accurate measurement of the amount of endotoxin that contaminates thermolysin is required. The present invention addresses the problem of providing a novel measurement method which enables accurate measurement of the amount of endotoxin that contaminates thermolysin. The present invention also addresses the problem of providing thermolysin containing a reduced amount of contaminant thermolysin, and the use thereof. There is provided thermolysin containing contaminant endotoxin in an amount of 1 EU/mg or less. There is also provided a method for measuring endotoxin that contaminates thermolysin, the method including pretreatment of deactivating the thermolysin. An enzyme preparation including the thermolysin according to the present invention as an active ingredient has a high utility value in the field of regenerative medicine.

The present invention is directed to a method for manufacturing an enzyme preparation, comprising at least one recombinant Actinoallomurus endopeptidase with glutenase activity, at high yields and suitable for human use. The invention is further directed to a recombinant expression vector for expressing the recombinant endopeptidase(s) of interest, and to a S. lividans host cell comprising said vector. Moreover, the present invention is directed the enzyme preparation obtained by said method, to formulations of the same and to clinical uses thereof.

The present invention is directed to a method for manufacturing an enzyme preparation, comprising at least one recombinant Actinoallomurus endopeptidase with glutenase activity, at high yields and suitable for human use. The invention is further directed to a recombinant expression vector for expressing the recombinant endopeptidase(s) of interest, and to a S. lividans host cell comprising said vector. Moreover, the present invention is directed the enzyme preparation obtained by said method, to formulations of the same and to clinical uses thereof.

The present invention relates to a novel endoprotease, mutants thereof having binding but lacking or having reduced hydrolyzing activity, and use in methods of studying and isolating O-linked glycoproteins.

The present invention relates to a novel endoprotease, mutants thereof having binding but lacking or having reduced hydrolyzing activity, and use in methods of studying and isolating O-linked glycoproteins.

Described are compositions, in particular lyophilizates, containing proteolytic enzymes, and methods for producing the compositions. Typically these compositions contain one or more proteases with collagenase activity and a neutral protease, for example, thermolysin. The compositions are free of acetate salts. Surprisingly, such compositions can be dissolved in water more rapidly than lyophilized protease mixtures of the state of the art.

Described are compositions, in particular lyophilizates, containing proteolytic enzymes, and methods for producing the compositions. Typically these compositions contain one or more proteases with collagenase activity and a neutral protease, for example, thermolysin. The compositions are free of acetate salts. Surprisingly, such compositions can be dissolved in water more rapidly than lyophilized protease mixtures of the state of the art.

A truncated and modified Serratiopeptidase or a variant thereof, and polynucleotides encoding the same. The truncated and modified Serratiopeptidase may have an amino acid sequence including amino acids 1 to 344, and amino acids 1 to 380 of SEQ ID NO: 1. The truncated and modified Serratiopeptidase may further include a first Cysteine (C) residue at a N-terminus of the truncated and modified Serratiopeptidase, substituted for at least one of Alanine 8 and Leucine 12 of SEQ ID NO: 1; and a second Cysteine residue at a C-terminus of the truncated and modified Serratiopeptidase, substituted for at least one of Valine 339 and Arginine 302 of SEQ ID NO: 1. The first and the second Cysteine residues may be adapted to form at least one disulfide bond including at least one of C8-C339, and C12-C302 disulfide bonds between the N-terminus and the C-terminus of the truncated and modified Serratiopeptidase.