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WO2010058679A1 - Promoteur de la réduction de fracture - Google Patents

Promoteur de la réduction de fracture Download PDF

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Publication number
WO2010058679A1
WO2010058679A1 PCT/JP2009/068295 JP2009068295W WO2010058679A1 WO 2010058679 A1 WO2010058679 A1 WO 2010058679A1 JP 2009068295 W JP2009068295 W JP 2009068295W WO 2010058679 A1 WO2010058679 A1 WO 2010058679A1
Authority
WO
WIPO (PCT)
Prior art keywords
milk
basic protein
fracture repair
fraction
fracture
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Ceased
Application number
PCT/JP2009/068295
Other languages
English (en)
Japanese (ja)
Inventor
城戸瑞穂
渡辺敏之
檀上敦
田中輝男
上辻大輔
小野愛子
芹澤篤
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Kyushu University NUC
Snow Brand Milk Products Co Ltd
Original Assignee
Kyushu University NUC
Snow Brand Milk Products Co Ltd
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Kyushu University NUC, Snow Brand Milk Products Co Ltd filed Critical Kyushu University NUC
Priority to US13/129,613 priority Critical patent/US20120040908A1/en
Priority to JP2010539192A priority patent/JPWO2010058679A1/ja
Priority to AU2009318621A priority patent/AU2009318621A1/en
Priority to CA2743406A priority patent/CA2743406A1/fr
Publication of WO2010058679A1 publication Critical patent/WO2010058679A1/fr
Anticipated expiration legal-status Critical
Ceased legal-status Critical Current

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Classifications

    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K35/00—Medicinal preparations containing materials or reaction products thereof with undetermined constitution
    • A61K35/12—Materials from mammals; Compositions comprising non-specified tissues or cells; Compositions comprising non-embryonic stem cells; Genetically modified cells
    • A61K35/20—Milk; Whey; Colostrum
    • A—HUMAN NECESSITIES
    • A21—BAKING; EDIBLE DOUGHS
    • A21D—TREATMENT OF FLOUR OR DOUGH FOR BAKING, e.g. BY ADDITION OF MATERIALS; BAKING; BAKERY PRODUCTS
    • A21D2/00—Treatment of flour or dough by adding materials thereto before or during baking
    • A21D2/08—Treatment of flour or dough by adding materials thereto before or during baking by adding organic substances
    • A21D2/24—Organic nitrogen compounds
    • A21D2/26—Proteins
    • A21D2/261—Animal proteins
    • A21D2/263—Animal proteins from dairy products
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; MAKING OR TREATMENT THEREOF
    • A23C19/00—Cheese; Cheese preparations; Making thereof
    • A23C19/06—Treating cheese curd after whey separation; Products obtained thereby
    • A23C19/068—Particular types of cheese
    • A23C19/08—Process cheese preparations; Making thereof, e.g. melting, emulsifying, sterilizing
    • A23C19/082—Adding substances to the curd before or during melting; Melting salts
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
    • A23J1/00—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
    • A23J1/20—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from milk, e.g. casein; from whey
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23K—FODDER
    • A23K20/00—Accessory food factors for animal feeding-stuffs
    • A23K20/10—Organic substances
    • A23K20/142—Amino acids; Derivatives thereof
    • A23K20/147—Polymeric derivatives, e.g. peptides or proteins
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
    • A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
    • A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
    • A23L33/17—Amino acids, peptides or proteins
    • A23L33/18—Peptides; Protein hydrolysates
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
    • A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
    • A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
    • A23L33/17—Amino acids, peptides or proteins
    • A23L33/19—Dairy proteins
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/01—Hydrolysed proteins; Derivatives thereof
    • A61K38/012—Hydrolysed proteins; Derivatives thereof from animals
    • A61K38/018—Hydrolysed proteins; Derivatives thereof from animals from milk
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P19/00—Drugs for skeletal disorders
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P19/00—Drugs for skeletal disorders
    • A61P19/08—Drugs for skeletal disorders for bone diseases, e.g. rachitism, Paget's disease
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
    • A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs

Definitions

  • the present invention relates to a fracture repair accelerator, a method for producing the same, a food and drink containing the fracture repair accelerator, and a feed.
  • the fracture repair-promoting agent of the present invention has an action of promoting multistage reactions such as inflammation, cartilage formation or subperiosteal bone formation, angiogenesis, and bone remodeling, which are repair reactions of fracture sites. Therefore, the fracture repair promoter of the present invention is useful for the treatment of fractures.
  • osteoporosis In recent years, with the aging of the population, bone-related risks such as osteoporosis and fractures tend to increase. In bone tissue, bone formation by osteoblasts and bone resorption by osteoclasts are constantly working in a well-balanced manner. However, the balance is not maintained and a disease that appears as a result of leaning to bone resorption is osteoporosis. In particular, in older women, the role of osteoclasts that resorb bone predominates after menopause due to the lack of estrogen secretion. To prevent osteoporosis, it is necessary to take measures to maintain bone mass. Vitamin D preparations and the like have been disclosed as pharmaceuticals for alleviating bone loss and fracture incidence in osteoporosis.
  • Non-Patent Document 1 Non-Patent Document 1
  • Non-Patent Document 2 Fracture healing occurs through processes such as inflammation, callus formation, collagen production of chondrocytes in the callus, angiogenesis, and bone remodeling.
  • bone formation is performed by the action of osteoblasts and only plays a part in the fracture healing process.
  • factors that affect osteoblast differentiation and proliferation include cbfa-1, FGF-1, FGF-2, milk-derived basic protein fractions, and the like (see, for example, Patent Document 1 and Non-Patent Document 3).
  • a fracture site When a bone is not able to withstand external forces and a fracture is caused, the fracture site is repaired through processes such as inflammation of the fracture site, formation of a callus, angiogenesis, and bone remodeling.
  • repairing a fracture site is a complex reaction in bone tissue including blood vessels and nerves. Therefore, it is unclear whether it has the effect of promoting the healing process of fracture, which is a complex reaction system, simply by promoting bone formation via osteoblasts.
  • the recovery of the fracture may not be accelerated. That is, the above-described substances are pharmacological actions only in the part of forming bones, and it is not clear whether a series of reactions for fracture repair is promoted.
  • an object of the present invention is to provide a fracture repair accelerator that accelerates repair of a fracture site by ingestion, a method for producing the same, a food and drink that contains the fracture repair accelerator, and a feed.
  • this invention is invention which consists of either of the following structures.
  • a fracture repair promoter comprising a milk-derived basic protein fraction as an active ingredient.
  • a fracture repair promoter comprising as an active ingredient a basic peptide fraction obtained by degrading the milk-derived basic protein fraction according to (1) or (2) with a proteolytic enzyme.
  • the proteolytic enzyme is at least one proteolytic enzyme selected from the group consisting of pepsin, trypsin and chymotrypsin.
  • Milk or a milk-derived raw material is brought into contact with a cation exchange resin to adsorb basic proteins, and a fraction adsorbed on the resin is eluted with an eluent having a salt concentration of 0.1 M to 1.0 M.
  • a method for producing a fracture repair accelerator comprising the obtained milk-derived basic protein fraction as an active ingredient.
  • Milk or a raw material derived from milk is brought into contact with a cation exchange resin to adsorb basic protein, and a fraction adsorbed on this resin is eluted with an eluent having a salt concentration of 0.1 M to 1.0 M to obtain
  • a method for producing a fracture repair accelerator comprising a basic peptide fraction obtained by degrading a milk-derived basic protein fraction with a proteolytic enzyme as an active ingredient.
  • the fracture repair accelerator of the present invention has a remarkable fracture repair action at the fracture site and is useful for the treatment of fractures due to external force, illness, and fatigue. Moreover, the fracture repair promoter of the present invention can be easily taken orally.
  • the fracture repair accelerator of the present invention is derived from milk and can be taken with peace of mind.
  • the feature of the fracture repair accelerator of the present invention is that a basic protein fraction derived from milk or a basic peptide fraction obtained by degrading a basic protein fraction with a proteolytic enzyme is used as an active ingredient.
  • This milk-derived basic protein fraction is obtained from milk of mammals such as cow's milk, human milk, goat milk, sheep milk, and this basic peptide fraction is a milk-derived basic protein fraction. It is obtained by acting a proteolytic enzyme on the bone, and has the effect of promoting the repair of the fracture site. Based on these actions, the treatment of fractures can be accelerated.
  • the milk-derived basic protein fraction used as an active ingredient of this fracture repair accelerator has the following properties. 1) According to Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis (SDS-PAGE), it consists of several proteins having a molecular weight in the range of 3,000-80,000. 2) 95% by weight or more is protein and contains a small amount of other fat and ash. 3) Protein mainly consists of lactoferrin and lactoperoxidase. 4) The amino acid composition of the protein contains 15% by weight or more of basic amino acids such as lysine, histidine and arginine.
  • SDS-PAGE Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis
  • Such a basic protein fraction is obtained by, for example, bringing a milk material such as skim milk or whey into contact with a cation exchange resin to adsorb the basic protein, and the basic protein fraction adsorbed on this resin is reduced to 0.00. Elution with 1M-1.0M salt eluate, collect this elution fraction, desalinate and concentrate by reverse osmosis (RO) membrane, electrodialysis (ED) method, etc., and dry as necessary Can be obtained.
  • RO reverse osmosis
  • ED electrodialysis
  • a method for obtaining a protein fraction by elution with an eluent exceeding pH 5 and an ionic strength exceeding 0.5 Japanese Patent Laid-Open No. 5-202098
  • a method using alginate gel Japanese Patent Laid-Open No. 61-246198]
  • a method of obtaining from whey using inorganic porous particles Japanese Patent Laid-Open No. 1-86839
  • a method of obtaining from milk using a sulfated ester compound Japanese Patent Laid-Open No. 63-255300
  • the basic protein fraction obtained by such a method can be used.
  • the basic peptide fraction derived from milk has the same amino acid composition as the basic protein fraction.
  • pepsin, trypsin, and the basic protein fraction derived from milk obtained by the above method are used. It can be obtained as a peptide composition having an average molecular weight of 4,000 or less by allowing a proteolytic enzyme such as chymotrypsin to act, and further allowing a proteolytic enzyme such as pancreatin to act as necessary.
  • the active ingredient milk-derived basic protein fraction or basic peptide fraction can be used as it is, but according to conventional methods, powders and granules It can be formulated into tablets, capsules, drinks and the like. Furthermore, since these basic protein fractions and basic peptide fractions are relatively heat-stable, the raw material containing the milk-derived basic protein or basic peptide fraction is usually used under the conditions used. Heat sterilization is also possible.
  • the dose of the fracture repair accelerator of the present invention varies depending on the age, therapeutic effect, disease state, etc., but may be ingested about 10 to 500 mg per day. Moreover, what is necessary is just to be able to mix
  • the basic protein fraction and basic peptide fraction of the present invention no acute toxicity was observed in rats. Moreover, it is desirable that the basic protein fraction and the basic peptide fraction of the present invention be taken orally together with a calcium salt having good absorbability. Examples of such a calcium salt having good absorbability include calcium chloride, calcium carbonate, calcium lactate, eggshell, milk-derived calcium-containing material, and the like.
  • a column (diameter 5 cm ⁇ height 30 cm) packed with 400 g of a cation exchange resin sulfonated chitopearl (Fujibo Co., Ltd.) was thoroughly washed with deionized water, and then 40 liters of unsterilized skim milk (pH 6. 7) was passed at a flow rate of 25 ml / min. After passing through the column, the column was thoroughly washed with deionized water, and the basic protein fraction adsorbed on the resin was eluted with 0.02 M carbonate buffer (pH 7.0) containing 0.98 M sodium chloride.
  • 0.02 M carbonate buffer pH 7.0
  • the eluate was desalted with a reverse osmosis (RO) membrane, concentrated, and lyophilized to obtain 21 g of a powdery basic protein fraction.
  • This basic protein fraction can be used as it is as a fracture repair accelerator of the present invention.
  • Example 1 When the basic protein fraction obtained in Example 1 was measured by sodium dodecyl sulfate-polyacrylamide (SDS-PAGE) electrophoresis, the molecular weight was distributed in the range of 3,000-80,000.
  • SDS-PAGE sodium dodecyl sulfate-polyacrylamide
  • Example 2 The component composition of the basic protein fraction obtained in Example 1 was analyzed. The results are shown in Table 1. As shown in this table, most of this fraction is protein.
  • Example 3 The protein composition of the basic protein fraction obtained in Example 1 was analyzed. The results are shown in Table 2. This basic protein fraction contains 40% by weight or more of lactoferrin and lactoperoxidase.
  • Example 4 The basic protein fraction obtained in Example 1 was hydrolyzed with 6N hydrochloric acid at 110 ° C. for 24 hours, and then the amino acid composition was analyzed with an amino acid analyzer (L-8500 type, manufactured by Hitachi, Ltd.). The results are shown in Table 3. This basic protein fraction contains 15% by weight or more of basic amino acids in the amino acid composition.
  • An acidic polysaccharide gel made of carrageenan was processed into beads (Japanese Unexamined Patent Publication No. 61-246198), and a column (diameter 100 cm ⁇ height 20 cm) packed with 50 kg was sufficiently washed with deionized water. 3000 liters of skim milk (pH 6.7) was passed through this column at a flow rate of 25 ml / min. After passing through the column, the column was thoroughly washed with deionized water, and the basic protein fraction adsorbed on the resin was eluted with 0.02 M carbonate buffer (pH 7.0) containing 1.5 M sodium chloride.
  • the eluate was desalted with a reverse osmosis (RO) membrane, concentrated, and lyophilized to obtain 136 g of powdery basic protein fraction powder.
  • This basic protein fraction can be used as it is as a fracture repair accelerator of the present invention.
  • the right tibia was not subjected to a fracture, and a needle was inserted into the medullary cavity to form a sham operation group. After confirming awakening after the operation, administration of the basic protein fraction was started.
  • the experiment was conducted as three groups: a non-administration group (CTRL), a 0.165% administration group, and a 1% administration group.
  • CTRL non-administration group
  • the basic protein fraction was administered orally and in a form dissolved in drinking water. In order to prevent spoilage, the basic protein fraction was replaced with a new one every two days.
  • the evaluation of fracture repair was 4 weeks after the operation. The mice were perfused and fixed during deep anesthesia, photographed with soft X-rays (Softex, Tokyo), and then ⁇ CT was photographed to evaluate the fracture recovery state.
  • the biomechanical analysis measured the mechanical strength of the tibia 4 weeks after using the electronic measurement control type precision universal material testing machine (autograph). The measurement item evaluated total energy (toughness: resistance to failure, total area of stress-s
  • FIG. 1 shows soft X-ray images (4 weeks after surgery) of mouse fracture models in the group not administered with the basic protein fraction (CTRL) and the group administered with 1%. From the results of FIG. 1, it was revealed that the bone density around the fracture line was higher in the basic protein fraction administration group.
  • CTRL basic protein fraction
  • FIG. 2 shows a ⁇ CT image of a mouse fracture model. Areas showing high BMD (Bone Mineral Density) values are shown in warm colors, and areas showing low BMD values are shown in cold colors. The fracture site is indicated by a white arrow. In the basic protein fraction administration group, the area around the fracture site showed high BMD, and the fracture repair tended to be clearly promoted.
  • BMD Battery Mineral Density
  • FIG. 3 shows the total energy representing bone toughness. It was revealed that administration of the basic protein fraction increased the total energy as compared to the basic protein fraction non-administered group (CTRL). Moreover, in the 1% basic protein fraction administration group, a significantly high value was shown. Therefore, it was revealed that the group to which the basic protein fraction was administered promoted fracture repair compared to the non-administered group. In addition, although the experimental result was not shown, the same effect was recognized when the basic peptide fraction obtained in Example 4 and Example 5 was used.
  • CTRL basic protein fraction non-administered group
  • Example 1 Each component was mixed with the composition shown in Table 4, and pressure-molded to prepare a tablet having a fracture repair-promoting action containing the milk-derived basic protein fraction obtained in Example 1.
  • Example 1 After mixing each component with the composition shown in Table 6 and filling it in a container, it is heat sterilized to prepare a jelly having a fracture repair promoting action containing the milk-derived basic protein fraction obtained in Example 1 did.
  • Each component was mixed with the composition shown in Table 7, emulsified at an emulsification temperature of 85 ° C., and a process cheese having a fracture repair promoting action containing the milk-derived basic protein fraction obtained in Example 1 was prepared. .
  • Example 1 Each component was mixed with the composition shown in Table 9, and a feed for breeding dogs having a fracture repair promoting action containing the milk-derived basic protein fraction obtained in Example 1 was prepared.

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  • Medicines Containing Material From Animals Or Micro-Organisms (AREA)

Abstract

L'invention porte sur une substance capable de favoriser la réduction d'une partie fracturée dans une fracture provoquée par une force extérieure, une fatigue ou une maladie. L'invention porte également sur un procédé de production de la substance. L'invention porte en outre sur un produit capable de favoriser la réduction d'une fracture, tel qu'un aliment, une boisson et un apport alimentaire comprenant le promoteur de réduction de fracture. L'invention porte spécifiquement sur un promoteur de réduction de fracture comprenant, en tant qu'ingrédient actif, une fraction contenant une protéine basique issue du lait. Dans le promoteur, la fraction contenant la protéine basique issue du lait est produite par mise en contact d'une matière première du lait ou issue du lait avec une résine échangeuse de cations afin de provoquer l'adsorption de la protéine basique par la résine échangeuse de cations et par élution de la fraction adsorbée sur la résine au moyen d'un éluent ayant une concentration en sel de 0,1 à 1,0 mole.
PCT/JP2009/068295 2008-11-18 2009-10-19 Promoteur de la réduction de fracture Ceased WO2010058679A1 (fr)

Priority Applications (4)

Application Number Priority Date Filing Date Title
US13/129,613 US20120040908A1 (en) 2008-11-18 2009-10-19 Fracture repair promoter
JP2010539192A JPWO2010058679A1 (ja) 2008-11-18 2009-10-19 骨折修復促進剤
AU2009318621A AU2009318621A1 (en) 2008-11-18 2009-10-19 Fracture repair promoter
CA2743406A CA2743406A1 (fr) 2008-11-18 2009-10-19 Promoteur de la reduction de fracture

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
JP2008-294445 2008-11-18
JP2008294445 2008-11-18

Publications (1)

Publication Number Publication Date
WO2010058679A1 true WO2010058679A1 (fr) 2010-05-27

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PCT/JP2009/068295 Ceased WO2010058679A1 (fr) 2008-11-18 2009-10-19 Promoteur de la réduction de fracture

Country Status (5)

Country Link
US (1) US20120040908A1 (fr)
JP (1) JPWO2010058679A1 (fr)
AU (1) AU2009318621A1 (fr)
CA (1) CA2743406A1 (fr)
WO (1) WO2010058679A1 (fr)

Cited By (11)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2013132675A1 (fr) * 2012-03-09 2013-09-12 雪印メグミルク株式会社 Agent de renforcement osseux
WO2014020684A1 (fr) * 2012-07-31 2014-02-06 雪印メグミルク株式会社 Fromage et son procédé de production
JPWO2014020677A1 (ja) * 2012-07-31 2016-07-11 雪印メグミルク株式会社 飲料及びその製造方法
JPWO2014020680A1 (ja) * 2012-07-31 2016-07-11 雪印メグミルク株式会社 発酵乳類及びその製造方法
JPWO2014020679A1 (ja) * 2012-07-31 2016-07-11 雪印メグミルク株式会社 発酵乳類及びその製造方法
JPWO2014020678A1 (ja) * 2012-07-31 2016-07-11 雪印メグミルク株式会社 飲料及びその製造方法
JP2016152809A (ja) * 2016-04-05 2016-08-25 雪印メグミルク株式会社 飲料及びその製造方法
JP2017121249A (ja) * 2017-02-28 2017-07-13 雪印メグミルク株式会社 飲料及びその製造方法
JP2017123859A (ja) * 2017-02-28 2017-07-20 雪印メグミルク株式会社 発酵乳類及びその製造方法
JP2017123860A (ja) * 2017-02-28 2017-07-20 雪印メグミルク株式会社 発酵乳類及びその製造方法
JP2017137266A (ja) * 2016-02-04 2017-08-10 雪印メグミルク株式会社 軟骨機能改善剤

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* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP6395350B2 (ja) * 2013-03-28 2018-09-26 雪印メグミルク株式会社 筋萎縮防止剤

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JPH08151331A (ja) * 1994-09-30 1996-06-11 Snow Brand Milk Prod Co Ltd 骨強化剤
JPH09191858A (ja) * 1996-01-23 1997-07-29 Snow Brand Milk Prod Co Ltd 塩基性タンパク質組成物、塩基性ペプチド組成物及びその利用
WO2000078351A1 (fr) * 1999-06-18 2000-12-28 Mitsubishi Pharma Corporation Promoteurs de l'osteogenese
JP2002370982A (ja) * 2001-06-12 2002-12-24 Kowa Co 骨形成促進剤

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JP2008214237A (ja) * 2007-03-02 2008-09-18 Snow Brand Milk Prod Co Ltd Ｒａｎｋｌ産生抑制剤
WO2008111573A1 (fr) * 2007-03-12 2008-09-18 Snow Brand Milk Products Co., Ltd. Stimulateur de sécrétion d'hormone de croissance
CA2704144C (fr) * 2007-11-01 2015-12-29 Megmilk Snow Brand Co., Ltd. Matiere alimentaire favorisant la differenciation d'un osteoblaste et inhibant la differenciation d'un osteoclaste

Patent Citations (4)

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Publication number Priority date Publication date Assignee Title
JPH08151331A (ja) * 1994-09-30 1996-06-11 Snow Brand Milk Prod Co Ltd 骨強化剤
JPH09191858A (ja) * 1996-01-23 1997-07-29 Snow Brand Milk Prod Co Ltd 塩基性タンパク質組成物、塩基性ペプチド組成物及びその利用
WO2000078351A1 (fr) * 1999-06-18 2000-12-28 Mitsubishi Pharma Corporation Promoteurs de l'osteogenese
JP2002370982A (ja) * 2001-06-12 2002-12-24 Kowa Co 骨形成促進剤

Non-Patent Citations (2)

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US20120040908A1 (en) 2012-02-16
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