The Green Cross Corporation

Sumitomo Electric Industries, Limited

Sumitomo Electric Sintered Alloy, Ltd.

Yoshitomi Pharmaceutical Industries, Ltd.

Mitsubishi Pharma Corporation

Tao Health Life Pharma Co., Ltd.

Munehiro Noda

Takao Ohmura

Akinori Sumi

Kazumasa Yokoyama

Wataru Ohtani

Kaeko Kamide

Kazuya Takeshima

Naoto Furuhata

Kazuhiro Oohara

Syoichi Ishikawa

Masahide Kondo

Tomoyuki Ishimine

Kazunari Shimauchi

Nagatoshi Fujiwara

Tomoyuki Ueno

Michio Sato

Koji Naito

Satoshi Horie

Shigeki Egashira

Hajime Horii

Shoji Ideno

Minako Hoshi

Naoto Fuluhata

Takayuki Tashiro

A method for manufacturing a sintered gear comprising the steps of: preparing a cylindrical green compact; gear-cutting the green compact with a hob; and sintering the gear-hobbed green compact, wherein the hob is such that a ratio of a number of cutting edges thereof per round to a number of starts thereof exceeds 8.

Method for manufacturing sintered gear

A method of making a sintered body includes a step of preparing raw material powder containing powder of inorganic material, a step of producing a powder compact having a high-density portion with a relative density of 93% or more and a low-density portion with a relative density of less than 93% by compressing the raw material powder injected into a mold, a step of producing a machined compacted part by machining at least the high-density portion of the powder compact, and a step of sintering the machined compacted part to make a sintered body, wherein a perimeter shape of a cavity constituted by the mold in a cross-section perpendicular to an axial direction of the mold is such than a maximum stress applied to an inner perimeter surface of the mold during a compacting process using the mold is less than or equal to 2.6 times an imaginary maximum stress that is applied to an inner perimeter surface of an imaginary mold during a compacting process using the imaginary mold, the imaginary mold having an imaginary cavity that has a same area as the cavity and that has a circular perimeter shape.

Method of making sintered body, and powder compact

An antibody provided by the present invention has a low reactivity with amyloid precursor proteins, and has a higher reactivity with amylospheroids than with amyloid &#x3b2; fibrils or monomeric amyloid &#x3b2;-proteins. According to the present invention, an antibody is provided that has a higher reactivity with amylospheroids than with amyloid precursor proteins, and has any one or more of the following properties: (i) a higher activity with amylospheroids than with amyloid &#x3b2; fibrils; (ii) a higher reactivity with amylospheroids than with monomeric amyloid &#x3b2;-proteins; and (iii) an activity of inhibiting neuronal cell death induced by amylospheroids.

Antibody and use thereof

The invention provides a process for purifying recombinant human serum albumin (rHSA) by heating a-culture medium containing rHSA and the rHSA-producing host cells, feeding said heated solution upwardly into a fluidized bed in which adsorbent particles are suspended to effect contacting with the adsorbent particles and then recovering the adsorbed fraction containing the rHSA, and a composition comprising rHSA which shows a A350/A280 ratio of below 0.015, when formulated into a 25% solution of said albumin.

Process for purifying recombinant human serum albumin

Human serum albumin obtained by gene manipulation techniques can be purified by a combination of specified steps in which a culture supernatant obtained from a human serum albumin-producing host is subjected to ultrafiltration, heat treatment, acid treatment and another ultrafiltration, followed by subsequent treatments with a cation exchanger, a hydrophobic chromatography carrier and an anion exchanger, and by salting-out to thereby obtain a pure form of human serum albumin which contains substantially no proteinous and polysaccharide contaminants, which is formulated into a pharmaceutical preparation. The thus obtained human serum albumin can further be purified by treating recombinant human serum albumin with a hydrophobic chromatography carrier at pH of 2 to 5 and a salt concentration of 0.4 to 1 and exposing the carrier to a pH of 6 to 8 and a salt concentration of 0.01 to 0.3 M, or treating the culture supernatant with boric acid or a salt thereof at pH 8 to 11 for 1 to 10 hours and recovering the supernatant. This process makes it possible to effeciently purify recombinant human serum albumin and to provide substantially pure human serum albumin which does not contain producer host-related substances and other contaminants and is sufficiently free from coloration.

Recombinant human serum albumin, process for producing the same and

The invention provides a process for purifying recombinant human serum albumin (rHSA) by heating a culture medium containing rHSA and the rHSA-producing host cello, feeding said heated solution upwardly into a fluidized bed in which adsorbent particles are suspended to effect contacting with the adsorbent particles and then recovering the adsorbed fraction containing the rHSA, and a composition comprising rHSA which shows a A35D/A280 ratio of below 0.015, when formulated into a 25% solution of said albumin.

A method for decoloring a recombinant human serum albumin by treating the albumin with a reducing agent is disclosed. Also, a method for decoloring a recombinant human serum albumin by treating the albumin with a method removing free polysaccharides with a cation exchanger followed by heat treatment is disclosed. The present invention provides a recombinant human serum albumin, coloring of which is fully suppressed by preventing binding of certain coloring components, which are contained in the raw materials or contaminants secreted by a microorganism, to human serum albumin so as not to cause coloring of the human serum albumin.

Method for decoloring human serum albumin

Human serum albumin obtained by gene manipulation techniques can be purified by a combination of specified steps in which a culture supernatant obtained from a human serum albumin-producing host is subjected to ultrafiltration, heat treatment, acid treatment and another ultrafiltration, followed by subsequent treatments with a cation exchanger, a hydrophobic chromatography carrier and an anion exchanger, and by salting-out to thereby obtain a pure form of human serum albumin which contains substantially no proteinous and polysaccharide contaminants, which is formulated into a pharmaceutical preparation. This process makes it possible to effeciently purify recombinant human serum albumin and to provide substantially pure human serum albumin which does not contain producer host-related substances and other contaminants and is sufficiently free from coloration.

Growing community of inventors

Osaka, Japan

Munehiro Noda