Abstract: A polypeptide cleavage method characterized in that arginine or lysine is at the P1 position of a desired cleavage site in a polypeptide, an amino acid other than aspartic acid, glutamic acid or proline is at the P1? position, a single basic amino acid or two or three consecutive basic amino acids are situated at any site in the amino acid sequence from the P10 position to the P3 position or from the P3? position to the P5? position (with the proviso that a single basic amino acid is not situated at the P6 or P4 position), and OmpT protease or its variant enzyme having a substitution at the 97th amino acid from the N-terminus is used to cleave the desired cleavage site in the polypeptide.

Abstract: Disclosed are: a recombinant C-terminal ?-amidated enzyme derivative which lacks the formation of at least one disulfide bond among five disulfide bonds occurring in a C-terminal ?-amidated enzyme derived from Xenopus laevis; DNA encoding the derivative; an expression vector carrying the DNA; a bacterium Escherichia coli transformed with the expression vector; and a method for producing the derivative by using the bacterium Escherichia coli.

Abstract: Disclosed are: a recombinant C-terminal ?-amidated enzyme derivative which lacks the formation of at least one disulfide bond among five disulfide bonds occurring in a C-terminal ?-amidated enzyme derived from Xenopus laevis; DNA encoding the derivative; an expression vector carrying the DNA; a bacterium Escherichia coli transformed with the expression vector; and a method for producing the derivative by using the bacterium Escherichia coli.

Abstract: The present invention provides a transformed cell which is transformed by at least one gene of enzymes participating in biosynthesis of tetrahydrobiopterin and a process for the production of a biopterin compound using the same. In accordance with the present invention, the biopterin compound can be produced in large quantities in an industrial advantageous manner from less expensive materials.

Abstract: A method for reducing the formation of a byproduct polypeptide containing an O-acetylserine residue in place of a serine residue by adding at least one of histidine, methionine or glycine to the medium in a method for producing a polypeptide containing a serine residue by culturing transformed cells, and a method for producing a polypeptide containing a serine residue by culturing transformed cells, characterized by reducing the formation of a byproduct polypeptide containing an O-acetylserine residue in place of a serine residue by adding at least one of histidine, methionine or glycine to the medium.

Abstract: Methods of using OmpT protease are provided. In particular, the invention provides for a method of controlling cleavage of a polypeptide by OmpT protease comprising, converting a sequence site comprising two arbitrary consecutive amino acids and/or amino acid(s) in the vicinity of the site in the polypeptide into other amino acids; which method comprises setting lysine or arginine as the amino acid at the ?1-position concerning the site and setting a specific amino acid as the amino acid at the +1-position; and/or setting specific amino acid(s) as the amino acid(s) at the ?4-position and/or the ?6-position relative to the site; so that a desired part of the polypeptide is cleaved by OmpT protease and/or an undesired part of the polypeptide is not (or hardly) cleaved by OmpT protease. A method of producing a target polypeptide is also provided.

Abstract: A polypeptide cleavage method characterized in that arginine or lysine is at the P1 position of a desired cleavage site in a polypeptide, an amino acid other than aspartic acid, glutamic acid or proline is at the P1? position, a single basic amino acid or two or three consecutive basic amino acids are situated at any site in the amino acid sequence from the P10 position to the P3 position or from the P3? position to the P5? position (with the proviso that a single basic amino acid is not situated at the P6 or P4 position), and OmpT protease or its variant enzyme having a substitution at the 97th amino acid from the N-terminus is used to cleave the desired cleavage site in the polypeptide.

Abstract: The present invention provides a transformed cell which is transformed by at least one gene of enzymes participating in biosynthesis of tetrahydrobiopterin and a process for the production of a biopterin compound using the same. In accordance with the present invention, the biopterin compound can be produced in large quantities in an industrial advantageous manner from less expensive materials.

Abstract: The present invention provides a transformed cell which is transformed by at least one gene of enzymes participating in biosynthesis of tetrahydrobiopterin and a process for the production of a biopterin compound using the same. In accordance with the present invention, the biopterin compound can be produced in large quantities in an industrial advantageous manner from less expensive materials.

Abstract: A process for the production of a desired polypeptide comprising the steps of: (1) transforming host cells with an expression vector comprising a gene coding for a fusion protein comprising a desired polypeptide and a protective polypeptide; (2) culturing the transformed host cells so as to express said gene to produce a fusion protein; and (3) excising the desired polypeptide from the fusion protein with a protease intrinsic to the host cells. According to the present invention, a large amount of a desired polypeptide can be produced at a low cost. Especially according to the present invention, a large amount of S. aureus V8 protease can be efficiently produced at low cost using a safe host such as E. coli according to gene recombination procedures.

Abstract: Kex2 protease derivatives obtained by transforming methanol-assimilating with expression vectors containing DNA coding for any amino acid sequence which is an amino acid sequence of Kex2 protease wherein the N-terminus is the Met at position 1 and the C-terminus is one of the amino acids between positions 618 (inclusive) and 698 (inclusive), or a modification of that amino acid sequence, culturing the resulting transformants and recovering the derivatives from the cultures, as well as gene systems coding for the derivatives and a method for producing the Kex2 protease derivatives using the gene systems. Also, a method for excision of desired peptides using the Kex2 protease derivatives.

Abstract: Mutant proteases are obtained with one or more mutation sites in the natural V8 protease protein, and with enzyme activities even in the presence of high urea concentrations.Inactivation of enzyme activity is minimized even in the presence of high concentrations of urea, to thus allow lower amounts of enzyme to be added to urea-containing reaction systems and shorten reaction times. As an additional advantage, the ability to cleave proteins in the presence of high urea concentrations makes it possible to obtain hitherto unobtainable peptide fragments.

Abstract: The present invention is a process to express a target peptide in a large amount and accumulate the target peptide in host cells in the form of inclusion bodies. The process comprises:A) culturing host cells transformed with a plasmid able to express a gene coding for a fusion protein represented in the formula A--L--B, wherein B is a target peptide, A is a protective peptide comprising a 90-210 amino acid fragment E. coli .beta.-galactosidase, and L is a linker peptide positioned between the C-terminus of the protective peptide and the N-terminus of the target peptide and selected so that when the fusion protein is treated by an enzyme or chemical substance, the target peptide is separated, and wherein the protective peptide and linker peptide are selected so that the isoelectric point of the fusion protein in between 4.9 and 6.

Abstract: A lactose repressor protein wherein at least one amino acid at the position of 94, 241, 265 or 300 in the wild lactose repressor is replaced with an amino acid other than that of the wild lactose repressor, and the use thereof.The present mutant lactose repressor represses the expression of a desired gene at 30.degree. C. or lower temperature, and induces the expression of a desired gene at 37.degree. C. or higher temperature, and therefor can control the expression by change of a culture temperature without using an expensive inducer such as IPTG.

Abstract: An outer metal jacket for a dry cell, prepared by butting a rectangular metal plate at both side edges and joining the butted part by welding or bonding to make a cylindrical body, characterized in that a part having smaller mechanical strength is integrally provided on at least one of the upper and lower rims of the cylindrical body as a safety mechanism. When the inner pressure is increased by any reason originated from an electrochemical cell system accommodated therein, the safety mechanism is opened outwardly and the increased pressure is reduced therethrough.