Abstract: A predictor 62 predicts a future of a prediction target in a traffic area. The predictor 62 includes a movement state information acquirer 620 configured to acquire movement state information, a surrounding state information acquirer 621 configured to acquire surrounding state information, a traffic environment information acquirer 622 configured to acquire traffic environment information, a driver state information acquirer 623 configured to acquire driver state information, a traffic scene specifier 624 configured to specify a traffic scene on the basis of the movement state information, the surrounding state information, and the traffic environment information, an action pattern selector 625 configured to select, as a predicted action pattern, at least one from among a plurality of predetermined action patterns on the basis of the traffic scene and the driver state information, and an action predictor 626 configured to predict future action on the basis of the predicted action pattern.

Abstract: The object of the present invention is to provide a glycosylated polypeptide having uniform sugar chain structure which has interferon ? activity. It was found that a glycosylated polypeptide having uniform sugar chain structure as well as having interferon ? activity can be prepared by a method comprising a step of synthesizing a glycosylated peptide fragment and at least two peptide fragments and a step of linking the glycosylated peptide fragment and the at least two peptide fragments.

Abstract: The object of the present invention is to provide a polypeptide having interferon ? activity glycosylated with highly uniform sialylated sugar chains. The present invention is a glycosylated polypeptide, wherein the polypeptide is any polypeptide selected from the group consisting of the following (1) to (4); (1) a polypeptide consisting of the amino acid sequence represented by SEQ ID NO. 1, (2) a polypeptide having one or a few amino acids deleted, substituted, or added in the polypeptide consisting of the amino acid sequence represented by SEQ ID NO. 1, (3) a polypeptide that is an analog of interferon ?, and (4) a polypeptide having 80% or more homology to the polypeptide consisting of the amino acid sequence represented by SEQ ID NO. 1, in which amino acids at 4 to 6 locations are substituted with glycosylated amino acids, and wherein all of the non-reducing terminals of said sugar chain are sialylated.

Abstract: The object of the present invention is to provide a polypeptide having interferon ? activity glycosylated with highly uniform sialylated sugar chains. The present invention is a glycosylated polypeptide, wherein the polypeptide is any polypeptide selected from the group consisting of the following (1) to (4); (1) a polypeptide consisting of the amino acid sequence represented by SEQ ID NO. 1, (2) a polypeptide having one or a few amino acids deleted, substituted, or added in the polypeptide consisting of the amino acid sequence represented by SEQ ID NO. 1, (3) a polypeptide that is an analog of interferon ?, and (4) a polypeptide having 80% or more homology to the polypeptide consisting of the amino acid sequence represented by SEQ ID NO. 1, in which amino acids at 4 to 6 locations are substituted with glycosylated amino acids, and wherein all of the non-reducing terminals of said sugar chain are sialylated.

Abstract: A process for chemically converting a peptide chain into a peptide thioester includes, when a —C(?X)—R1 group is introduced to the thiol group of the cysteine residue and then the resulting peptide is reacted with a compound having a leaving group represented by the formula: —NH—C(?Y)NHR3 in an organic solvent, the —NH—C(?Y)NHR3 group binds via addition reaction to the carboxyl group of the N-terminal-side peptide bond of the cysteine residue, whereby the peptide bond is cleaved and the C-terminal-side peptide fragment is cut off. Further, when the resulting peptide chain having the —NH—C(?Y)NHR3 group is reacted with a thiol in a buffer solution, a thiol exchange reaction occurs, namely, the thiol group of the thiol binds to the carbonyl carbon to which the —NH—C(?Y)NHR3 group has bound, whereby the —NH—C(?Y)NHR3 group is eliminated.

Abstract: The object of the present invention is to provide a glycosylated polypeptide having uniform sugar chain structure which has interferon ? activity. It was found that a glycosylated polypeptide having uniform sugar chain structure as well as having interferon ? activity can be prepared by a method comprising a step of synthesizing a glycosylated peptide fragment and at least two peptide fragments and a step of linking the glycosylated peptide fragment and the at least two peptide fragments.

Abstract: A process for chemically converting a peptide chain into a peptide thioester includes, when a —C(?X)—R1 group is introduced to the thiol group of the cysteine residue and then the resulting peptide is reacted with a compound having a leaving group represented by the formula: —NH—C(?Y)NHR3 in an organic solvent, the —NH—C(?Y)NHR3 group binds via addition reaction to the carboxyl group of the N-terminal-side peptide bond of the cysteine residue, whereby the peptide bond is cleaved and the C-terminal-side peptide fragment is cut off. Further, when the resulting peptide chain having the —NH—C(?Y)NHR3 group is reacted with a thiol in a buffer solution, a thiol exchange reaction occurs, namely, the thiol group of the thiol binds to the carbonyl carbon to which the —NH—C(?Y)NHR3 group has bound, whereby the —NH—C(?Y)NHR3 group is eliminated.

Abstract: The present invention provides a method for producing a peptide, characterized in that it comprises converting an —SH group of a peptide comprising an amino acid residue having the —SH group to an —OH group, wherein said method comprises the following steps (a) to (c): (a) allowing an —SH group in a peptide to react with a methylating agent to convert the —SH group to an -SMe group; (b) allowing the -SMe group obtained in the step (a) to react with a cyanizing agent to produce a reaction intermediate; and (c) converting the reaction intermediate obtained in the step (b) to a peptide comprising an amino acid residue having an —OH group under more basic conditions than the conditions in the step (b).

Abstract: The present invention provides a method for producing a peptide, characterized in that it comprises converting an —SH group of a peptide comprising an amino acid residue having the —SH group to an —OH group, wherein said method comprises the following steps (a) to (c): (a) allowing an —SH group in a peptide to react with a methylating agent to convert the —SH group to an -SMe group; (b) allowing the -SMe group obtained in the step (a) to react with a cyanizing agent to produce a reaction intermediate; and (c) converting the reaction intermediate obtained in the step (b) to a peptide comprising an amino acid residue having an —OH group under more basic conditions than the conditions in the step (b).

Abstract: Oligosaccharide chain added GLP-1 peptides are more stable in blood and more active in controlling blood-sugar levels than GLP-1 peptides without added oligosaccharides. Oligosaccharide chain added GLP-1 peptides having GLP-1 activity include at least one or at least two amino acids each substituted with an oligosaccharide chain added amino acid in GLP-1; a peptide having the amino acid sequence of GLP-1 with deletion, substitution or addition of one or several amino acids; or a GLP-1 analog. Oligosaccharide chain added GLP-1 peptides with at least one amino acid substituted with an oligosaccharide chain added amino acid include an oligosaccharide chain with oligo hyaluronic acid. Oligosaccharide chain added amino acids include oligosaccharide chains attached to amino acids via linkers.

Abstract: A process for chemically converting a peptide chain into a peptide thioester includes, when a —C(?X)—R1 group is introduced to the thiol group of the cysteine residue and then the resulting peptide is reacted with a compound having a leaving group represented by the formula: —NH—C(?Y)NHR3 in an organic solvent, the —NH—C(?Y)NHR3 group binds via addition reaction to the carboxyl group of the N-terminal-side peptide bond of the cysteine residue, whereby the peptide bond is cleaved and the C-terminal-side peptide fragment is cut off. Further, when the resulting peptide chain having the —NH—C(?Y)NHR3 group is reacted with a thiol in a buffer solution, a thiol exchange reaction occurs, namely, the thiol group of the thiol binds to the carbonyl carbon to which the —NH—C(?Y)NHR3 group has bound, whereby the —NH—C(?Y)NHR3 group is eliminated.

Abstract: The present invention relates to an oligosaccharide chain added GLP-1 peptide that has higher stability in blood than that of GLP-1 and, preferably, exhibits higher activity of controlling blood-sugar levels than that of GLP-1. The present invention relates to an oligosaccharide chain added GLP-1 peptide having GLP-1 activity, wherein at least one amino acid is substituted with an oligosaccharide chain added amino acid, in: (a) GLP-1; (b) a peptide having the amino acid sequence of GLP-1 with deletion, substitution or addition of one or several amino acids; or (c) a GLP-1 analog.

Abstract: The present invention relates to an oligosaccharide chain added GLP-1 peptide that has higher stability in blood than that of GLP-1 and, preferably, exhibits higher activity of controlling blood-sugar levels than that of GLP-1. The present invention relates to an oligosaccharide chain added GLP-1 peptide having GLP-1 activity, wherein at least one amino acid is substituted with an oligosaccharide chain added amino acid, in: (a) GLP-1; (b) a peptide having the amino acid sequence of GLP-1 with deletion, substitution or addition of one or several amino acids; or (c) a GLP-1 analog.

Abstract: A process for chemically converting a peptide chain into a peptide thioester includes, when a —C(?X)—R1 group is introduced to the thiol group of the cysteine residue and then the resulting peptide is reacted with a compound having a leaving group represented by the formula: —NH—C(?Y)NHR3 in an organic solvent, the —NH—C(?Y)NHR3 group binds via addition reaction to the carboxyl group of the N-terminal-side peptide bond of the cysteine residue, whereby the peptide bond is cleaved and the C-terminal-side peptide fragment is cut off. Further, when the resulting peptide chain having the —NH—C(?Y)NHR3 group is reacted with a thiol in a buffer solution, a thiol exchange reaction occurs, namely, the thiol group of the thiol binds to the carbonyl carbon to which the —NH—C(?Y)NHR3 group has bound, whereby the —NH—C(?Y)NHR3 group is eliminated.

Abstract: The present invention relates to an oligosaccharide chain added GLP-1 peptide that has higher stability in blood than that of GLP-1 and, preferably, exhibits higher activity of controlling blood-sugar levels than that of GLP-1. The present invention relates to an oligosaccharide chain added GLP-1 peptide having GLP-1 activity, wherein at least one amino acid is substituted with an oligosaccharide chain added amino acid, in: (a) GLP-1; (b) a peptide having the amino acid sequence of GLP-1 with deletion, substitution or addition of one or several amino acids; or (c) a GLP-1 analog.

Abstract: Oligosaccharide chain added GLP-1 peptides are more stable in blood and more active in controlling blood-sugar levels than GLP-1 peptides without added oligosaccharides. Oligosaccharide chain added GLP-1 peptides having GLP-1 activity include at least one or at least two amino acids each substituted with an oligosaccharide chain added amino acid in GLP-1; a peptide having the amino acid sequence of GLP-1 with deletion, substitution or addition of one or several amino acids; or a GLP-1 analog. Oligosaccharide chain added GLP-1 peptides with at least one amino acid substituted with an oligosaccharide chain added amino acid include an oligosaccharide chain with oligo hyaluronic acid. Oligosaccharide chain added amino acids include oligosaccharide chains attached to amino acids via linkers.

Abstract: The present invention relates to an oligosaccharide chain added GLP-1 peptide that has higher stability in blood than that of GLP-1 and, preferably, exhibits higher activity of controlling blood-sugar levels than that of GLP-1. The present invention relates to an oligosaccharide chain added GLP-1 peptide having GLP-1 activity, wherein at least one amino acid is substituted with an oligosaccharide chain added amino acid, in: (a) GLP-1; (b) a peptide having the amino acid sequence of GLP-1 with deletion, substitution or addition of one or several amino acids; or (c) a GLP-1 analog.

Abstract: The present invention provides a method for producing a peptide, characterized in that it comprises converting an —SH group of a peptide comprising an amino acid residue having the —SH group to an —OH group, wherein said method comprises the following steps (a) to (c): (a) allowing an —SH group in a peptide to react with a methylating agent to convert the —SH group to an —SMe group; (b) allowing the —SMe group obtained in the step (a) to react with a cyanizing agent to produce a reaction intermediate; and (c) converting the reaction intermediate obtained in the step (b) to a peptide comprising an amino acid residue having an —OH group under more basic conditions than the conditions in the step (b).

Abstract: The present invention relates to an oligosaccharide chain added GLP-1 peptide that has higher stability in blood than that of GLP-1 and, preferably, exhibits higher activity of controlling blood-sugar levels than that of GLP-1. The present invention relates to an oligosaccharide chain added GLP-1 peptide having GLP-1 activity, wherein at least one amino acid is substituted with an oligosaccharide chain added amino acid, in: (a) GLP-1; (b) a peptide having the amino acid sequence of GLP-1 with deletion, substitution or addition of one or several amino acids; or (c) a GLP-1 analog.

Abstract: A hemostatic agent and method for preparation thereof are described, said hemostatic agent comprising a carrier in the shape of flake or fiber having thrombin and Factor XIII fixed thereto, wherein said carrier is composed of a biodegradable material having a water absorption capability of about 50 weight percent or more, said flake has a longer dimension of about 5000 microns or less, a shorter dimension of about 3000 microns or less, and a thickness of about 2000 microns or less, and said fiber has a single yarn fineness of about 30 deniers or less and a yarn length of about 10 mm or less.