CN1049456A - The preparation of animal fiber surgical adhesive - Google Patents
The preparation of animal fiber surgical adhesive Download PDFInfo
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- CN1049456A CN1049456A CN 89106463 CN89106463A CN1049456A CN 1049456 A CN1049456 A CN 1049456A CN 89106463 CN89106463 CN 89106463 CN 89106463 A CN89106463 A CN 89106463A CN 1049456 A CN1049456 A CN 1049456A
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- compound method
- liquid
- animal
- fibrinogen
- globulin
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- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Abstract
The invention discloses a kind of compound method of surgery animal fiber surgical adhesive.Utilization is saltoutd, absorption, isoelectric precipitation, low-temperature precipitation method are extracted from animal blood slurry and lung tissue and prepared biological adhesive.Main component has thrombinogen, thromboplastinum, Fibrinogen, albumin and globulin (and aprotinin).Be made into A, B two liquid during use, splash into simultaneously in the wound, utilize the agglutination between each composition that edge of wound is clung.This binding agent has carried out the antigenicity processing, is used for human body and can cause immunoreation.A large amount of zooperies and clinical practice result show that bonding incision operation is easy; Post-operation inflammatory is light, nothing infects, healing is fast; Stay visible cicatrix after the healing hardly.Can be used for binding skin, gastrointestinal, uterus, blood vessel, nerve, muscle, fat, and be used for hemostasis, ophthalmology, otology of essence organ pipe etc.
Description
The present invention relates to a kind of compound method that is used for operating glue (animal fibrinogen complex biological adhesive).
Complexity when traditional surgical operation is sewed up not only operating cost, and suture material often causes tissue inflammation, infection suppurates, tuberosity hypertrophy, fistula, edge of wound cracking or ischemic necrosis, and organa parenchymatosum's damage etc.Therefore, people are making great efforts always untiringly for a long time, seek for a kind of ideal biological adhesive to replace suture.
Up to now, forefathers try exhausted chemical biological adhesive and mainly contain epoxy resin, acroleic acid resin, polyurethane, polystyrene, cyanoacrylate, polymethacrylates etc.Absorb but these chemical substances are extremely difficult in vivo, and have certain toxic and side effects.
Except that chemical substance, people also tried out the albumen biological adhesive.Mainly contain gelatin, mussel glue and human fibrin binding agent.Wherein preceding two kinds because of causing allergic reaction and separate the hard to tackle practical value of not having, and the latter once was widely used clinically.But human fibrin binding agent system extracts from human plasma, not only extracts tissue-derived shortage, costs an arm and a leg, and the potential danger of propagating hepatitis B, syphilis and AIDS human diseasess such as (AIDS) is arranged.Therefore in the use that has been under an embargo of some country.
The invention reside in to extract from animal tissue and prepared animal fibrinogen complex new bio binding agent, main component has thrombinogen, thromboplastinum, Fibrinogen, albumin, globulin and lime nitrate (or adding aprotinin).Except that lime nitrate was chemical reagent, all the other each compositions all extracted from animal tissue.Therefore its extraction is tissue-derived extensively, with low cost, and does not propagate the potential danger of human diseases.Owing in the leaching process each composition has been carried out the antigenicity processing, not only can be used for veterinary clinic but also can be used for the human body operation simultaneously.Its action principle is a polyreaction of utilizing the biological enzyme substrate to take place.
Thrombinogen in the binding agent is that methods such as employing is saltoutd, absorption, isoelectric precipitation are extracted from animal blood slurry.Leaching process is as follows:
A, Mg(OH)
2The preparation of Emulsion:
(1), NH
4OH(concentrates) 1000ml
（2）、20%MgCl4000ml
(1) is slowly added (2), and the limit edged stirs, and allows precipitate sink, the supernatant that inclines, and water washes precipitate repeatedly then.Through centrifugal, the 500g precipitate is suspended in the 1000ml water promptly.
The preparation of B, anticoagulant:
1.85% K
2C
2O
4.2H
2O
0.5% H
2C
2O
4.2H
2O
0.85% NaCl
C, fresh animal blood (cattle, pig, sheep etc.) 10000ml
Add anticoagulant 600ml
Earlier anticoagulant is added container, flow into animal blood 10000ml, use the centrifuge separated plasma behind the mixing immediately, 3000 rev/mins, 10 minutes.
D, second day morning added cold distilled water 1500ml dilution by every 100ml blood plasma, transfer PH to 4.5 with 1% acetic acid then, promptly produced precipitation through 3 hours.
E, anhydrate precipitate is centrifugal, add 3 liters of oxalates normal saline (0.5%K
2C
2O4+0.9%NaCl), add 0.1N NaOH PH is transferred to 6.4, the precipitate dissolving.
F, will go up add 1000mlMg(OH in the liquid)
2Emulsion, room temperature left standstill 30 minutes, and taking precipitate is centrifugal to anhydrate.
G, precipitate is dissolved in 1.5 premium on currency logical CO
2(2.5 atmospheric pressure) concussion 30 minutes transforms Mg(OH)
2Be magnesium carbonate.
H, buchner funnel elimination precipitate, the dress bag filter was dialysed in distilled water three days.
I, the solution that will dialyse are transferred PH to 6.5, centrifugal removal inactive protein with 1% acetic acid.Supernatant is transferred PH to 4.5 with 1% acetic acid, and the centrifugal precipitate that obtains promptly contains abundant thrombinogen.Precipitate is dissolved in the 100ml0.1% oxalates normal saline, transfers PH to 7.0, cryopreservation with 0.1N NaOH.
Thromboplastinum in the binding agent be with saltout, absorption method extracts from animal lung tissue, leaching process is as follows:
The fresh pulverizing lung tissue of A, every 100g adds the 100ml normal saline, stirs frequently and places 48 hours.
B, extracting centrifugal liquid add 20mlMg(OH with one times of normal saline dilution, the such liquid of every 120ml)
2Emulsion absorption impurity.
C, will go up liquid centrifuging and taking supernatant, every 100ml supernatant adds the saturated (NH of 100ml
4)
2SO
4Solution.The supernatant of leaving away once more is dissolved in normal saline with precipitate.
It is capable centrifugal again that D, last liquid add the saturated sulphuric acid amine aqueous solution of equivalent, removes supernatant, and precipitate is dissolved in the 15ml normal saline.
E, last liquid dress bag filter are extremely removed (NH fully with normal saline dialysis
4)
2SO
4Till, gained solution promptly contains abundant thromboplastinum.
Fibrinogen in the binding agent, albumin and globulin are all produced from animal blood slurry, and process is as follows:
It is centrifugal that A, fresh animal blood 10000ml add anticoagulant 600ml mixing, and 3000 rev/mins, 10 minutes, separated plasma.
B, blood plasma that separation is obtained made K cryogenic treatment in 12 hours placing below-80 ℃.
C, the blood plasma after the freezing processing is melted, transfer PH to 5.5 with 1% acetic acid, the centrifugal precipitate that obtains is dissolved in the 500ml normal saline, wherein contains a large amount of Fibrinogens, albumin and globulin.Content can record with photoelectric colorimetry or electrophoresis method.
After each composition of binding agent makes, all be placed on below-80 ℃ to preserve and re-use more than 24 hours, to reduce its antigenicity.
In order to prolong storage life, each composition lyophilization can be preserved.
Before binding agent uses, earlier each one-tenth is distributed into A liquid and B liquid.
The preparation of A liquid:
Get prothrombin solution 10ml, add thromboplastinum solution 5ml, heat to 37 ℃, 10 minutes, thrombinogen promptly was converted into thrombin.Can record thrombin amount with standard fibers protein liquid or Ox blood plasma.According to purposes, be diluted to 100-3000KIU/ml with normal saline, add lime nitrate simultaneously, content is 50-250mmol/ml.Prepare back 4 ℃ of preservations.
The preparation of B liquid:
Get Fibrinogen, albumin and globulin solution (or freeze-dried product), with the normal saline dilution, according to purposes, content is respectively Fibrinogen 50-200Mg/ml, and albumin 20-100mg/ml and globulin 50-200mg/ml prepare back 4 ℃ of preservations.
During use, inhale A liquid, each 0.5ml of B liquid with the 1ml needle tubing, heat to 37 ℃, equivalent splashes in the wound simultaneously.Agglutination takes place after mixing in each composition immediately.The patient draws close edge of wound alignment applying light about 5 seconds rapidly, and edge of wound promptly is stuck.10 centimeters long skin incisions approximately need the 0.2ml binding agent.
Prolong binding agent absorption in vivo and action time as need, can in B liquid, add aprotinin 1000-3000KIU/ml.Aprotinin has commodity product(s), also can own extract from animal tissue.In order to strengthen anti-infection ability, also can in B liquid, add antibacterials.
A large amount of zooperies and clinical practice result show that it is easy and simple to handle to sew up the incision with the bonding otch ratio of the animal fiber surgical adhesive among the present invention, can make operating time shorten 5-10 doubly; Post-operation inflammatory is light, does not have and infects, heals soon, all reaches the healing of first phase first class; The visible scar of the healing several no naked eyes in back shows many-sided superiority.This binding agent not only can binding skin, and can bonding muscle, fat, nerve, blood vessel, gastrointestinal, uterus and be used for hemostasis, ophthalmology, otology of organa parenchymatosum etc.
Claims (10)
1, a kind of compound method that is used for the biological adhesive of animal and human's body operation, it is characterized in that main component thrombinogen, thromboplastinum, Fibrinogen, albumin, globulin (and aprotinin) all extract from animal tissue, extract after K cryogenic treatment, liquid state or lyophilization are preserved, and the B liquid that is made into the A liquid that contains thrombin, lime nitrate and contains Fibrinogen, albumin and globulin (or adding aprotinin) uses.
2, press the compound method of binding agent in the claim 1, it is characterized in that except that lime nitrate, all the other each compositions all extract from animal tissue.
3, press compound method in the claim 1, it is characterized in that thrombinogen, Fibrinogen, albumin and globulin all extract from animal blood slurry.
4, press compound method in the claim 1, it is characterized in that thromboplastinum extracts from animal lung tissue.
5, press compound method in the claim 1, it is characterized in that each composition of binding agent extracts after re-use after-80 ℃ of following K cryogenic treatment.
6, press compound method in the claim 1, it is characterized in that the lime nitrate concentration in the A liquid is 50-250mmol/ml, concentration of thrombin is 100-3000KIU/ml.
7, press compound method in the claim 1, it is characterized in that the fibrinogen concentration in the B liquid is 50-200mg/ml, albumin concentration is that 20-100mg/ml and globulin concentration are 50-200mg/ml.
8, press compound method in the claim 1, when it is characterized in that using, A liquid and B liquid are heated to 37 °-39 ℃, equivalent splashes in the wound simultaneously.
9, press compound method in the claim 1, it is characterized in that binding agent can liquidly preserve or the solid-state preservation of cold drying.
10, by the compound method in the claim 1, it is characterized in that and in B liquid, to add aprotinin 1000-3000KIU/ml to prolong its action time.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN 89106463 CN1049456A (en) | 1989-08-12 | 1989-08-12 | The preparation of animal fiber surgical adhesive |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN 89106463 CN1049456A (en) | 1989-08-12 | 1989-08-12 | The preparation of animal fiber surgical adhesive |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CN1049456A true CN1049456A (en) | 1991-02-27 |
Family
ID=4856743
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN 89106463 Pending CN1049456A (en) | 1989-08-12 | 1989-08-12 | The preparation of animal fiber surgical adhesive |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN1049456A (en) |
Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0650512A1 (en) * | 1992-07-06 | 1995-05-03 | CryoLife, Inc. | Aldehyde-cured proteinaceous adhesive |
| CN101890181A (en) * | 2010-06-12 | 2010-11-24 | 广州倍绣生物技术有限公司 | Swine fibrin glue powder inhalation and preparation method and application thereof |
| CN104109203A (en) * | 2013-04-16 | 2014-10-22 | 宿松县春润食品有限公司 | Method for simple, convenient and industrialized purification of porcine fibrinogen |
-
1989
- 1989-08-12 CN CN 89106463 patent/CN1049456A/en active Pending
Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0650512A1 (en) * | 1992-07-06 | 1995-05-03 | CryoLife, Inc. | Aldehyde-cured proteinaceous adhesive |
| EP0650512A4 (en) * | 1992-07-06 | 1996-03-06 | Nicholas Kowanko | Aldehyde-cured proteinaceous adhesive. |
| CN101890181A (en) * | 2010-06-12 | 2010-11-24 | 广州倍绣生物技术有限公司 | Swine fibrin glue powder inhalation and preparation method and application thereof |
| CN101890181B (en) * | 2010-06-12 | 2014-04-30 | 广州倍绣生物技术有限公司 | Swine fibrin glue powder inhalation and preparation method and application thereof |
| CN104109203A (en) * | 2013-04-16 | 2014-10-22 | 宿松县春润食品有限公司 | Method for simple, convenient and industrialized purification of porcine fibrinogen |
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| Date | Code | Title | Description |
|---|---|---|---|
| C06 | Publication | ||
| PB01 | Publication | ||
| C10 | Entry into substantive examination | ||
| SE01 | Entry into force of request for substantive examination | ||
| C01 | Deemed withdrawal of patent application (patent law 1993) | ||
| WD01 | Invention patent application deemed withdrawn after publication |