Classifications

• • A—HUMAN NECESSITIES
  • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
  • A61L—METHODS OR APPARATUS FOR STERILISING MATERIALS OR OBJECTS IN GENERAL; DISINFECTION, STERILISATION OR DEODORISATION OF AIR; CHEMICAL ASPECTS OF BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES; MATERIALS FOR BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES
  • A61L26/00—Chemical aspects of, or use of materials for, wound dressings or bandages in liquid, gel or powder form
  • A61L26/0057—Ingredients of undetermined constitution or reaction products thereof
• • 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
  • A61K35/56—Materials from animals other than mammals
  • A61K35/57—Birds; Materials from birds, e.g. eggs, feathers, egg white, egg yolk or endothelium corneum gigeriae galli
• • 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
• • A—HUMAN NECESSITIES
  • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
  • A61L—METHODS OR APPARATUS FOR STERILISING MATERIALS OR OBJECTS IN GENERAL; DISINFECTION, STERILISATION OR DEODORISATION OF AIR; CHEMICAL ASPECTS OF BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES; MATERIALS FOR BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES
  • A61L26/00—Chemical aspects of, or use of materials for, wound dressings or bandages in liquid, gel or powder form
  • A61L26/0009—Chemical aspects of, or use of materials for, wound dressings or bandages in liquid, gel or powder form containing macromolecular materials
  • A61L26/0028—Polypeptides; Proteins; Degradation products thereof
  • A61L26/0047—Specific proteins or polypeptides not covered by groups A61L26/0033 - A61L26/0042

Definitions

• my medical protein hydrolysate comprises the soluble polypeptides and soluble amino acid constituents of immature animal protein such as chicken feet and its mineral content, resulting from the hydrolyzing of t animal protein with a dilute acid, preferably a weak organic acid such as acetic acid, and the subsequent drying, or con centrating, of the resulting solution.
• a dilute acid preferably a weak organic acid such as acetic acid
• the process comprises first cleansing the raw material, such as the feet of eight or nine week old broiler then comminuting this raw material and subjecting it to a dilute acid, under controlled pH and temperature conditions.
• the resulting solution is decanted, strained or filtered and then spray dried or otherwise dewatered or concentrated to a dry powder or dried gel.
• the powder is topically applied to a moist open wound, or is reconstituted with water and injected, wit a syringe, into the area to be treated.
• the gel is used for the treatment of relatively dry areas and can be reconstitut from the dry powder or from partially dried gel.
• I preferably used the feet of freshly killed im ⁇ mature broilers as my raw material and extract therefrom, polypeptides and amino acids that are lacking in antigenic properties.
• I make up a water solution of glacial acetic acid by adding the glacial acetic acid to the water to produce a first dilute acetic acid solution con ⁇ taining from about 1% to about 1-1/2% by weight, glacial acetic acid.
• This initial treatment or pretreatment with acetic acid solution is to remove blood, free fats and serum.
• the pH may run from pH 6.5 to pH 3.6 if desired.
• the washed comminuted feet mix is then added to this second solution in a one to one ratio by weight and the resulting mix is heated to a temperature of between 130°F and 140°F an constantly stirred for about 30-40 minutes, but it can be comingled and heated for a shorter period of time, with a de ⁇ crease in yield.
• This solubilized mixture is then decanted or drawn off and sent through a centrifuge to remove most of the fat and particulate matter.
• the defatted centrifuged solution is then passed through a filter. So far, I have found that the best filter bed to use is "Speed Flow" diatomaceous earth, though I am sure there are other filters that would be equall effective.
• the powder has an average particle size of fro about 1 micron to about 20 microns.
• a first extraction was made up by.mixing glacial acetic acid and water to produce a resulting solution having about 1% by weight, glacial acetic acid.
• the centrifuged solution was filtered by being passed through diatomaceous earth (Speed Flow - a Dow Chemical [Grefco] product). At this stage the solution was clear solution containing approximately 5.7 pounds of the polypeptides and amino acids mix.
• the clear solutio at a temperature of from about 100°F to about 120°F was pass through a spray dryer.
• the inlet temperature of the air was about 250°F and the outlet temperature was about 120°F.
• the resulting non-antigenic protein hydrolysate powder, being hydroscopic, was then immediately placed in an air tight, moisture impervious container so that it would not cake.
• Example I The procedure of Example I was repeated but instead of spray drying, the filtered solution was dried in dry air at a temperature of from 65° to 75°F, until it contained about 5%, by weight, moisture.
• the resulting protein hydrolysate material weighed 6.1 pounds and was placed in an airtight, moisture impervious container.
• the material was later mixed with water to produce various samples of gels containing from about 15% to about 30%, by weight, of the material.
• the water was preheated to from about 120°F to about 130°F and the material added to the warm water.
• the gels were kept under refrigeration.
• Example I a Sharpless centrifuge or cream separator with fixed parts was used.
• a Bowen spray dryer was used in Example I.
• My protein hydrolysate is particularly useful for the treatment of burns, particularly third degree burns.
• T dry powder is sprinkled over the affected area and combines with the moisture in the tissue to provide a protective cel stimulating coating.
• the gel is preferably used for first and second degree burns, where a relatively dry area is in ⁇ volved. Pain is usually stopped in three to five minutes after application to the affected area. I have found it preferable to apply a sprinkled layer of dry powder or gel to the burned area about every third day.
• the powder all for the fiberblasts or regenerative cells to continue to gro out from the center and edges of the wound so that skin gra ing is materially reduced or entirely eliminated. Further ⁇ more, the new skin even appears to be formed from normal cel and hair actually grows from the new skin in a normal way.
• the first cat was treated with protein hydrolysate prepared according to Example II above. Its wounds healed in 21 days without complications. It walked without a limp in 7 days.
• a third cat was treated with a prior art protein hydrolysate, hydrolysed casein, a Borden product. It developed hyperplasia on the 7th day and a secondary infection, both of which persisted until final healing at 33 days. This cat limped until final healing.
• the third and fourth cats also exhibited progressive atrophy of the muscles posterior to the incision continuing until the femur could be palpitated.
• the therapeutic agent of the present invention i.e., my medical protein hydrolysate
• my medical protein hydrolysate is hydroscopic mixture of polypeptides and amino acids. It appears to have the fantastic ability to create, around a wound area, conditions that allow true tissue regeneration, this in the total absence of antibodies, even in the most critically infected wounds.
• the wound is heavily covered with my powder or gel.
• my powder or gel When powder is used, the area must be moist that the powder can stick. No adverse tissue reaction has been observed in any treatment using my Protein Hydrolysate.

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• Health & Medical Sciences (AREA)
• Life Sciences & Earth Sciences (AREA)
• Chemical & Material Sciences (AREA)
• Epidemiology (AREA)
• Animal Behavior & Ethology (AREA)
• General Health & Medical Sciences (AREA)
• Public Health (AREA)
• Veterinary Medicine (AREA)
• Engineering & Computer Science (AREA)
• Materials Engineering (AREA)
• Medicinal Chemistry (AREA)
• Pharmacology & Pharmacy (AREA)
• Chemical Kinetics & Catalysis (AREA)
• Zoology (AREA)
• Bioinformatics & Cheminformatics (AREA)
• Immunology (AREA)
• Proteomics, Peptides & Aminoacids (AREA)
• Medicines Containing Material From Animals Or Micro-Organisms (AREA)
• Peptides Or Proteins (AREA)
• Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)

Applications Claiming Priority (2)

Publications (2)

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• 1976
  • 1976-05-10 US US05/685,050 patent/US4094973A/en not_active Expired - Lifetime
• 1978
  • 1978-06-12 WO PCT/US1978/000014 patent/WO1980000059A1/en unknown
  • 1978-06-12 CH CH123880A patent/CH642262A5/fr not_active IP Right Cessation
  • 1978-06-12 DE DE2857532A patent/DE2857532C1/de not_active Expired
• 1980
  • 1980-01-29 EP EP19790900610 patent/EP0018976A4/de not_active Withdrawn

Non-Patent Citations (1)

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