Product Description
PureCol®-S collagen is provided as a standard for use in assays where ultra-pure collagen is required.PureCol®-S collagen standard is approximately 97% Type I collagen with the remainder being comprised of Type III collagen. It contains a high monomer content as measured by gel permeation chromatography. This product is supplied at approximately a 3 mg/ml concentration. The concentration is confirmed by Biuret protein determination assay. The concentration for each specific lot is provided on a Certificate of Analysis that is available with the purchase of each product.PureCol®-Sis soluble atelo-collagen in 0.01 N HCI, therefore, the pH is approximately 2.0.
PureCol®-S is ideal for using as a collagen standard in controlled testing and assay procedures.PureCol®-Sis sterile filtered and is supplied as a ready to use solution.
Parameter, Testing, and Method | PureCol®-S Collagen Standard #5015 |
Sterilization Method | Filtration |
Extraction Method | Enzyme - atelocollagen |
Form | Solution |
Package Size | 20 mL |
Storage Temperature | 2-10°C |
Shelf Life | Minimum of 6 months from date of receipt |
Collagen Concentration - Biuret | 2.9-3.2 mg/mL |
Collagen Concentration - AAA | 2.9-3.2 mg/mL |
Collagen Purity - Silver Staining | >99.9% |
pH | 1.9-2.1 |
Kinetic Gel Test (Minutes) | <40 |
Gel Formation Tube Test (Minutes) | <40 |
Fibrillogenesis(Absorbance Units) | >0.5 |
Electrophoretic Pattern - Coomassie Blue | Characteristic |
Sterility - USP modified | No growth |
Endotoxin -LAL | <1.0 EU/mL |
Osmolality (mOsmo H2O/kg) | <35 |
Source | Bovine Hide |
Hydrogel Young's Modulus E (Pa) | Characteristic |
Directions for Use
Download the full PDF versionor continue reading below:
Coating Procedure
Note: Use these recommendations as guidelines to determine the optimal coating conditions for your culture system.
- Remove required quantity of collagen from the bottle and dispense into a dilution vessel.
- Dilute PureCol®-S in water to ~50 to 100 µg/ml (~1:30). A 0.01 N HCl solution may also be used.
- Swirl contents gently until material is completely mixed.
- Add appropriate amount of diluted PureCol®-S material to the culture surface ensuring that the entire surface is coated.
- Incubate at room temperature, covered, for 1-2 hours. Aspirate any remaining material. Alternatively, incubate at room temperature until surface is dry.
- Rinse coated surfaces carefully with sterile medium or PBS, avoid scratching surfaces.
- Coated surfaces are ready for use. They may also be stored at 2-8°C damp or air dried if sterility is maintained.
3-D Gel Preparation Procedure
- Slowly add 1 part of chilled 10X PBS or 10X culture media to 8 parts of chilled collagen solution with gentle swirling.
- Adjust pH of mixture to 7.2–7.6 using sterile 0.1 M NaOH. Monitor pH adjustment carefully (pH meter, phenol red, or pH paper).
- Adjust final volume to a total of 10 parts with sterile water.
- To prevent gelation, maintain temperature of mixture at 2–10°C.
- To form gel, warm to 37°C. Allow approximately 90 to 120 minutes for gel formation.
Product Q & A
The purity of PureCol® collagen is determined by SDS-PAGE, sodium dodecyl sulfate polyacrylamide gel electrophoresis in conjunction with bacterial collagenase sensitivity and silver staining techniques with a method sensitivity of 99.9%. It was found that PureCol® collagen is 95 to 98% Type I collagen and the remainder being comprised of Type III collagen.
SDS polyacrylamide gel electrophoresis demonstrates the presence of alpha, beta and gamma components in an appropriate ratio of approximately 40:30:30, respectively. PureCol® collagen is a native collagen as judged by polarimetry and trypsin sensitivity although the product does contain a low percentage of collagen fragments or shortened helices.
Conclusion: With the test method sensitivity of 99.9% (SDS-PAGE gel electrophoresis in conjunction with bacterial collagenase sensitivity and silver staining techniques) and no other proteins present in the preparation, it can be concluded that the purity of the PureCol® collagen is 99.9%.
The viscosity of PureCol® is ~32 cp.
PureCol® product has an isoelectric zone instead of isoelectric point. The isoelectric zone is pH 7 to 8. In addition, the collagen molecules in the PureCol® product will come out ofsolution starting at a pH above 5.5 and reach its plateau at pH 7 to 8 then gradually tapering off at pH 8 to 9.5.
Reduction of a commercially available, pepsin-solubilized, bovine dermal collagen (Vitrogen 100) (PureCol’s old product name) with sodium [3H]borohydride provided radiolabeled collagen preparations with specific activities ranging from 7.1-12.0 muCi/mg collagen. These specific activities were 2-3 times greater than those obtained by reduction of intact rat tail tendon collagen under similar conditions.
The alpha, beta, and higher aggregate components of type I collagen were radiolabeled as well as the alpha component of a small amount of type III collagen present in the samples. Fractionation of cyanogen bromide peptides showed that alpha 1(I)CB7, alpha 1(I)CB8, and alpha 2(I)CB3,5 were the predominant peptides labeled by this procedure. Amino acid analysis indicated that the majority of the radioactivity was in reducible cross-links, precursors of these cross-links, and in hexosyllysine residues.
Reconstitution experiments comparing this radiolabeled collagen with nonlabeled collagen showed them to be indistinguishable. Bacterial collagenase digestion of this reconstituted fibrillar collagen in both a lightly cross-linked (glutaraldehyde 0.0075%) and noncross-linked form provided evidence that digestion of labeled and nonlabeled collagens proceeded at similar rates. Thus, labeling did not change the properties of the collagen. Cross-linking made the preparation refractory to proteolytic degradation. Injection of fibrillar collagen preparations, spiked with radiolabeled collagen, into the guinea pig dermis followed by quantitation of the amount of radioactivity recovered from implant sites as a function of time, indicated that the lightly cross-linked samples also were more resistant to degradation in vivo than the noncross-linked preparation.
The half-life of noncross-linked collagen was about 4 days while that of the cross-linked collagen was about 25 days. These degradation rates were much faster than observed for similar, nonlabeled samples injected into the dermis of humans, presumably due to a higher metabolic activity in the guinea pig dermis.
Since the collagen in PureCol collagen contains approximately 95% Type I bovine collagen and 5% Type III bovine collagen, an anti-bovine collagen Type I antibody for your study can be used.
There is no difference. Vitrogen was the old tradename, and PureCol®is the new tradename.
We completed a study to show that DNA is completely destroyed at pH 2, and demonstrated that our collagen products do not contain DNA.
The collagen is fully hydrolyzed. The amino acid analysis is done using the Waters AccQ-Tag derivatization method.During the acid hydrolysis step, asparagine (N) is converted to aspartic acid (D) and glutamine (Q) is converted to glutamic acid (E). Tryptophan (W), if present, is destroyed during acid hydrolysis. Experimentally, one can determine the picomoles (pmol) of each amino acid per injected detected using amino acid standards.For the concentration determination, the total number of pmol of each amino acid is summed to get the total pmol of the 18 amino acids detected. The total pmol amino acids is divided by the theoretical number of amino acid residues in collagen based on the published sequence. The result is the pmol of collagen injected. The result is then multiplied by the dilution and 300,000 is used as the collagen molecular weight to get to mg/mL. The molecular weight of collagen is not well agreed upon.
Diluting with 1X PBS (rather than water or 0.01 N HCl) would have an effect for coating purposes. It would change the pH of the diluted collagen solution from acid to neutral pH. The pH change will transform the collagen molecules from a molecular form to a fibrillar form; and then the nature of coating surface will be changed from a monomeric coating to a fibrillar coating.
We use thefollowing antibodies from SouthernBiotech:
1. 1310-02 – Goat Anti-Type I Collagen-FITC
2. 1310-08 – Goat Anti-Type I Collagen-BIOT
3. 7100-05 – Streptavidin-HRP
The major collagen molecular species in our Type I collagen products are monomers (approx. 70%), but there are dimers, trimers and a few percentages of oligomers too (approx. 30%) with some minor amounts of collagen fragments. The collagen monomer is a rod shaped molecule with 300 nm in length and 1.5 nm in diameter. The dimer, trimer and oligomer are 600 nm, 900nm and even longer in length respectively. According to the coating procedures, the collagen molecules are attached to the charged polystyrene surface randomly by charge or affinity in acid conditions during the 1-2 hrs incubation period at 37°C, and any unattached materials are removed by aspiration and rinsing. Therefore, the coated surface is a single layer of collagen monomer, dimer, trimer and oligomer mixtures.The thickness of the mono-molecular layer is dependent on how those molecules are attached on the surface. The coating density thickness would generally be characterized as a 1 molecule thickness which could be ranging from a few nanometers to a few hundred nanometers with the whole surface being covered by collagen.
The net charge of Type I collagen products’ (PureCol®, Bovine Collagen and VitroCol®, Human Collagen) molecule is directly related to the pH. At an acidic pH, the amino acids (zwitterions) along the collagen molecule are positively charged, making the entire collagen molecule positive. At the isoelectric point (or zone) of collagen, around pH 7-8, the amino acids along the collagen molecule are positively and negatively charged, making the net charge of the collagen molecule close to zero. At a basic pH, the amino acids along the collagen molecule were negatively charged, making the entire collagen molecule negative.
Further, the nature of the charge of the collagen coating surface will be dependent on the type of coating applied. For a monomeric collagen coatings when the collagen is applied under an acidic pH condition, the surface is positively charged. If the surface is rinsed with pH neutral buffer or media then it will change the charge of the collagen surface net charge close to zero. For a 3D gel coating, the collagen prepared under neutral pH; the net charge of the collagen surface is close to zero.
Using rotary shadowing technique under transmission electron microscopy, it was found that our collagen, on average, consists of approximately 80% monomers, 13% dimers, trimers, and oligomers with the remaining 7% collagen fragments.
Yes.The collagen molecule in PureCol, Nutragen, VitroCol, and all of our other Atelo collagen products were prepared from native collagen matrix by pepsin treatment under controlled conditions to remove the non-helical portion, telo-peptides, only and the helical portion is intact. In this case, the enzymatic active sites for MMP (Matrix Metalloproteinase), such as for Mammalian Collagenase Matrix Metalloproteinase 8 (MMP-8), on the molecule was preserved.
These pepsin treated collagen products should behave as native intact collagen.
TGF beta would have been digested with the pepsin enzymatic digestion step. It was undetectable by SDS PAGE silver stain as well. We didn’t do any specific measurements by ELISA however but presences of TGF betais not anticipated.
We primarily use the Biuret method, but we also use BCA, AAA, and hydroxyl-proline assays.
- Collagen solutions that are frozen tend to have issues forming 3D hydrogels, and will likely not work. The solutions should still be good for 2D coatings.
- Collagen solutions that are left out at room temperature for extended periods of time may show signs of degradation, which will affect the formation of 3D hydrogels. It is likely still fine for 2D coatings.
Our recommendation is this: If you are using the product directly for a publication, we highly suggest buying a new bottle if the one you have was compromised.
Product References
Because PureCol® has been cited in over 2000 publications, we have only posted a few below:
Sorensen, Jacob R., et al. "An altered response in macrophage phenotype following damage in aged human skeletal muscle: implications for skeletal muscle repair."The FASEB Journal(2019): fj-201900519R.
Sorensen, Jacob R., et al. "An altered response in macrophage phenotype following damage in aged human skeletal muscle: implications for skeletal muscle repair."The FASEB Journal(2019): fj-201900519R.
Colaço, E., et al. "Hierarchical Collagen-Hydroxyapatite Nanostructures Designed Through Layer-by-Layer Assembly of Crystal-Decorated Fibrils."J., Hierarchical Collagen-Hydroxyapatite Nanostructures Designed Through Layer-by-Layer Assembly of Crystal-Decorated Fibrils (May 13, 2019)(2019).
Schwerdtfeger, Luke A., et al. "Human colon function ex vivo: Dependence on oxygen and sensitivity to antibiotic."PloS one14.5 (2019): e0217170.
Cardoso, Ana, et al. "MiR-144 overexpression as a promising therapeutic strategy to overcome glioblastoma cell invasiveness and resistance to chemotherapy."Human molecular genetics(2019).
Steele, Hannah E., et al. "Mechanotransduction of mitochondrial AMPK and its distinct role in flow-induced breast cancer cell migration."Biochemical and biophysical research communications514.2 (2019): 524-529.
Gehwolf, Renate, et al. "Global Responses of Il-1β-Primed 3D Tendon Constructs to Treatment with Pulsed Electromagnetic Fields."Cells8.5 (2019): 399.
Alexander, Frank, Sebastian Eggert, and Dorielle Price. "Label-Free Monitoring of 3D Tissue Models via Electrical Impedance Spectroscopy." (2019): 1-24.
Matysik-Woźniak, Anna, et al. "Examination of Kynurenine Toxicity on Corneal and Conjunctival Epithelium: In vitro and in vivo Studies."Ophthalmic research(2019): 1-12.
Compton, Clayton, et al. "Reconstitution of the Ventricular Endocardium Within Acellular Hearts."Regenerative Engineering and Translational Medicine(2019): 1-11.
Müller, A. L., et al. "4. Identification of miR-301a in Primary Human Atrial Fibroblasts and Bone Marrow-Derived Mesenchymal Progenitor Cells to Attenuate Endogenous Differentiation into Pro-Fibrotic Cells."Differentiation of Primary Human Pro-Fibrotic Mesenchymal Cells Influenced by Extracellular Matrix Environment Determined by Micro-RNA Expression(2018): 130.
Doblinger, Nina, et al. "Impact of hydroxyethyl starch and modified fluid gelatin on granulocyte phenotype and function."Transfusion(2019).
Elisabeth, et al. "Pro-Inflammatory Responses in Human Bronchial Epithelial Cells Induced by Spores and Hyphal Fragments of Common Damp Indoor Molds."International journal of environmental research and public health16.6 (2019): 1085.
Dodmane, Puttappa R., et al. "Biphasic changes in airway epithelial cell EGF receptor binding and phosphorylation induced by components of hogbarn dust."Experimental lung research44.10 (2018): 443-454.
McClellan, Alyce, et al. "A novel mechanism for the protection of embryonic stem cell derived tenocytes from inflammatory cytokine interleukin 1 beta."Scientific reports9 (2019).
Wang, Weiling, et al. "Aquaporin-3 deficiency slows cyst enlargement in experimental mouse models of autosomal dominant polycystic kidney disease."The FASEB Journal(2019): fj-201801338RRR.
Teo, Jye Yng, et al. "Surface tethering of stem cells with H2O2-responsive anti-oxidizing colloidal particles for protection against oxidation-induced death."Biomaterials201 (2019): 1-15.
Gehwolf, Renate, et al. "3D-Embedded Cell Cultures to Study Tendon Biology." (2019): 1-11.
Product Certificate of Analysis
Product Videos
How to Make 3D Collagen Hydrogels
Video
Seeding Collagen Gels with Cells
Video
30+ Type I Collagen Options
Video
Coating a Glass Coverslip with Collagen
Video
See More
Safety and Documentation
Safety Data Sheet
Certificate of Origin
Declaration of Material Source
Product Disclaimer
This product is for R&D use only and is not intended for human or other uses. Please consult the Material Safety Data Sheet for information regarding hazards and safe handling practices.
美国AdvancedBioMatrix(简称ABM) www.advancedbiomatrix.comAdvancedBioMatrix(简称ABM)是美国一家著名的生物公司,获得了AllerganInc的授权(Allergan用25年时间不断完善胶原蛋白相关的产品的生产工艺),将Allergan的专业和技术用于蛋白生产与检测,致力于为组织工程、细胞分析及细胞增殖等研究领域提供优质稳定的产品。AdvancedBioMatrix不断丰富已有产品线,目前可为三维细胞培养提供各种胶原蛋白、纤连蛋白、玻连蛋白、水性凝胶、不同粘度与分子量的透明质酸以及低代成纤维细胞等。在美国全部产品授权Sigma销售。AdvancedBioMatrix是组织培养,细胞分析和细胞增殖三维(3D)应用的生命科学领域的领导者。我们的产品被公认为纯度,功能性和一致性的标准。我们在生产,分离,纯化,冷冻干燥,细胞培养和蛋白质测试,粘附肽,附着因子,底物刚性和其他3D矩阵产品方面拥有丰富的专业知识。我们的专业技术和知识正在被用来确保我们的产品质量最高,批次之间一致且易于为我们的研究客户使用。
美国AdvancedBioMatrix是3D组织培养、细胞检测和细胞增殖等领域实验解决方案的佼佼者。AdvancedBioMatrix在分离、纯化、冻干、细胞培养和蛋白检测、多肽粘附、附着因子、基质硬度和其他3Dmatrix 产品开发方面有着丰富的经验。AdvancedBioMatrix的研发经验和专业知识确保其产品可达到最佳质量,并保证产品之间一致性,方便研究客户使用。以下为AdvancedBioMatrix3DMatrices 产品竞争优势:1. 提供高纯度和成分确定的胞外基质;2. 超过1000余篇文献引用PureCol产品,品质非常均一;3. 在3D培养基领域可提供最全面的产品线;4. 唯一可提供特异性刚性有机硅基板的公司(CytoSoft);5. 唯一可提供可溶性丝纤蛋白的供应商(可运用于多种3D培养);6. 如果客户首次接触3D胶原凝胶,AdvancedBioMatrix还是唯一的预制胶原蛋白(PureColEZGel)供应商;
以下产品为AdvancedBioMatrix全球畅销品:1.PureCol 牛源I型胶原蛋白 3mg/ml#5005-100ML2.Nutragen牛源I型胶原蛋白 6mg/ml#5010-50ML3.FibriCol 牛源I型胶原蛋白 10mg/ml#5133-20ML4.VitroCol 人源I型胶原蛋白 #5007-20ML5. 弹性蛋白原 #5052-1MG6.ECMSelectArraykitUltra-36#5170-1EA7.CytoSoft(刚性可变的基底,AdvancedBioMatrix最新添加产品5190-7EA)8. 人III型胶原蛋白 #5021-10MG9. 人IV型胶原蛋白 #5022-5MG10.SilkFibroin溶液 #5154-20ML11.Fibronectin#5080-5MG12.Vitronectin#5051-0.1MG
ebiomall.com
>
>
>
>
>
>
>
>
>
>
>
>
一、脑电图脑电图(EEG)检查:是在头部按一定部位放置8-16个电极,经脑电图机将脑细胞固有的生物电活动放大并连续描记在纸上的图形。正常情况下,脑电图有一定的规律性,当脑部尤其是皮层有病变时,规律性受到破坏,波形即发生变化,对其波形进行分析,可辅助临床对及脑部疾病进行诊断。对脑波的频率、波幅、两侧的对称性以及慢波的数量、部位、出现方式及有无病理波等进行分析。许多脑部病变可引起脑波的异常。如颅内占位性病变(尤其是皮层部位者)可有限局性慢波;散发性脑炎,绝大部分脑电图呈现弥漫性高波幅慢波;此外如脑血管病、炎症、外伤、代谢性脑病等都有各种不同程度的异常,但脑深部和线部位的病变阳性率很低。须加指出的是,脑电图表现没有特异性,必须结合临床进行综合判断,然而对于癫痫则有决定性的诊断价值,在阗痫发作间歇期,脑电图可有阵发性高幅慢波、棘波、尖波、棘一慢波综合等所谓“痛性放电”表现。为了提高脑电图的阳性率,可依据不同的病变部位采用不同的电极放置方法。如鼻咽电极、鼓膜电极和蝶骨电极,在开颅时也可将电极置于皮层(皮层电极)或埋入脑深部结构(深部电极);此外,还可使用各种诱发试验,如睁闭眼、过度换气、闪光刺激、睡眠诱发、剥夺睡眠诱发以及静脉注射美解眠等。但蝶骨电极和美解眠诱发试验等方法,可给病人带来痛苦和损害,须在有经验者指导下进行。随着科技的日益发展,近年来又有了遥控脑电图和24小时监测脑电图。
二、脑电地形图(BEAM)
是在EEG的基础上,将脑电信号输入电脑内进行再处理,通过模数转换和付立叶转换,将脑电信号转换为数字信号,处理成为脑电功率谱,按照不同频带进行分类,依功率的多少分级,最终使脑电信号转换成一种能够定量的二维脑波图像,此种图象能客观地反映各部电位变化的空间分布状态,其定量标志可以用数字或颜色表示,再用打印机打印在颅脑模式图上,或贮存在软盘上。它的优越性在于能发现EEG中较难判别的细微异常,提高了阳性率,且病变部位图象直观醒目,定位比较准确,从而客观对大脑机能进行评价。主要应用于缺血性脑血管病的早期诊断及疗效予后的评价,小儿脑发育与脑波变化的研究,视觉功能的研究,大浮肿瘤的定位以及精神药物的研究等。
三、脑磁图
电流在导体内流动进,导体周围可以产生磁场。同理,脑细胞的电活动也有极微弱的磁场,可用高灵敏度的磁场传感器予以检测,并记录其随时间变化的关系曲线,是即脑磁图,其图形与EEG图形相似。与EEG相比,优点是:可发现有临床意义而又不能被EEG记录到的波形,或检测到皮质局限性的异常电磁活动;此外,磁检器不与头皮接触,也减少了干扰造成的伪差。若与EEG同时描记,还可对不同物理方位的皮质群进行分析。但由于屏蔽、电磁装置以及其他设备复杂、昂贵,目前国内尚无此项设备。
四、诱发电位
给人体感官、感觉神经或运动皮质、运动神经以刺激,兴奋沿相应的神经通路向中枢或外周传导,在传导过程中,产生的不断组合传递的电位变化,即为诱发电位,对其加以分析,即或反映出不同部位的神经功能状态。由于诱发电位非常微小,须借助电脑对重复刺激的信号进行叠加处理,将其放大,并从淹没于肌电、脑电的背景中提取出来,才能加以描记。主要是对波形、主波的潜伏期、波峰间期和波幅等进行分析,为临床诊断提供参考,目前临床常用的有视觉、脑干听觉、体感、运动和事件相关诱发电位,以及视网膜图和耳蜗电图等,可分别反映视网膜、视觉通路、内耳、听神经、脑干、外周神经、脊髓后索、感觉皮质以及上下运动神经元的各种病变,事件相关诱发电位则用以判断患者的注意力和反应能力。诱发电位具有高度敏感性,对感觉障碍可进行客观评诂,对病变能进行定量判断。对心理精神领域可进行一定的检测,故当前广泛应用于对神经系统病变的早期诊断,病情随访,疗效判断,予后估计,神经系统发育情况的评估以及协助判断昏迷性质和脑死亡等。但图形无特异性,必须结合临床资料进行判断;不在有关神经传导径路中的病变,不能发现异常。近年,诱发电位的频谱分析和诱发电位地形图也在临床上逐渐开始应用,进一步提高了其临床应用价值。
五、肌电图(EMG)
是用肌电图仪记录神经和肌肉的生物电活动,对其波形进行测量分析,可以了解神经、肌肉的功能状态,协助对下运动神经元或肌肉疾病的诊断。目前常用的方法有三种:①针极肌电图:亦称普通肌电图,是将特制的针电极刺入肌腹,或用表面电极置于肌肉表面皮肤,在示波器上或记录纸上观察肌肉在静止、轻收缩、重收缩三种状态下的电位变化,以帮助判断疾病究系神经源性或肌源性损害。②神经传导速度测定:也即运动神经传导速度(MCV)和感觉神经传导速度(SCV)测定。系在神经干的近端(MCV)或远端(SCV)给以脉冲刺激,在远端效应肌(MCV)或近端神经走行部位(SCV)接收波形,测理两点之间的潜伏期和距离,即可计算出运动神经或感觉神经传导速度,主要用于了解神经传导功能情况。③其他:如重复频率试验,F波、H反射、牵张反射等检查以及单纤维肌电图检查等,可进一步了解神经、肌肉、神经一肌接头以及脊髓反射弧的功能状态。
六、脑阻抗血流图(REG)
是检查头部血管功能和供血情况的一种方法。其原理是通过放置在头部的电极给以微弱的高频电流,由于血液的电阻率最小,其电阻可随心动周期供血的变化而变化,这种节律性的阻抗变化,经血流图仪放大,可描记出波动性曲线,对其进行测量、计算、分析,可间接了解外周阻力、血管弹性和供血情况。本法简便易行,但因影响因素比较多,如情绪、气温、检查当时的血管功能状态等,故对其判断应加慎重。须结合临床症状,体征等进行判断。常用于脑动脉硬化、闭塞性脑血管病、偏头痛以及药物疗效观察等。
具体操作是:局麻下将3~4根电极导管经股静脉、锁骨下静脉送入冠状静脉窦、高位右心房及希氏束、右心室等部位,刺激心房和心室诱发与临床一致的心动过速,定位心动过速起源点,然后将消融用的电极导管送达已定位的起源点并与体外的射频发生器相连。放电后重复电生理检查,若不能诱发心动过速且临床随访无发作,则说明消融成功。
此方法治疗的疾病有:预激综合征和房室结双经路引起的阵发性室上性心动过速、房扑和房颤、室性心动过速及房性心动过速。
磁共振 CT 脑电图 多普勒 肌电图 诱发电位 脑脊液检查 血液检查。。。。。。。。。。。。
心内科
心脏电生理记录系统、有创血压监测系统、心脏射频消融仪、心电分析系统、多参数监护仪、医疗网络产品等。
产品主要用于心脏射频消融、心脏电生理检查、冠脉造影、经皮冠状动脉成型术、支架植入、二尖瓣球囊扩张等心脏介入手术;人体生理参数监测;心电图分析等
我们一般是在心导管室内,要在特殊的X线设备,可以转动的C臂心血管造影机,影像增强设备和电视荧屏设备,多导电生理记录仪,心脏程控刺激仪等。高档可以有三维电解剖生理定位标测系统比如CARTO,EnSite3000,这仅仅国内少数顶尖医院才有。
我们做电生理检查是通过你自身的血管放入心导管,直到心脏相应部位,一般主要局部麻醉,小孩则需要全麻。手术前必须停用抗心律失常药物至少5个半衰期以上,一般至少要3天,一般抗凝药物也是需要停用的。
我们局部需要手术前备皮,也就是局部皮肤清洁,有毛发的也需要清理干净。然后铺上洞巾。仅仅暴露局部血管穿刺部位。
我们穿刺血管插入诱发电极导管是根据不同需要来的,比如通常我们需要至少放置冠状静脉窦电极,右心室电极,高位右心房电极,和His束电极,那么冠状静脉窦电极是一般通过左锁骨下静脉或者右颈内静脉穿刺放置的,而右心室、高右房和His束电极则通过右股静脉放置。这些和体表心电图构成都可以让医生在电视屏幕上看到你不同的心电图图形,这样可以更加明确你心律失常的机制,部位。那么我们就可以标定你需要消融的部位(靶点)
我们通过插入电极导管,然后我们就进行心电生理检查,也就是人工给与各种电刺激,诱发你心律失常,比如我们可以采用输出电刺激信号比如用S1S1 刺激,也可以采用S1S2刺激等等,有时候可以静脉点滴异丙肾上腺素等药物,增加诱发的成功率,术前我们停用抗心律失常药物也是这个目的,就是诱发出你心律失常,这样我们根据体表和心内心电图,可以准确判断并定位你心律失常发生机制和部位,为下一步射频导管消融作准备,其实标定,是最为关键的一步,你只有找准敌人才能准确打击。准确的标定,也就是找准敌人的位置,那么就为打击敌人,做出关键的作用。我们的射频导管就像导弹一样,但是你必须先直到敌人在哪里,把它标定好,然后我们的导弹就可以直接定点清除。
目前比较新的高档的比如CARTO,就是类似于全球定位系统GPS的原理,可以准确三维立体定位你心律失常形成的部位和路径。一般我们针对最多是折返造成的心律失常,比如最多用于房室结双径路或者房室旁路引起的阵发性室上速,成功率一般是95%以上。
如果是房扑,主要是经典房扑,那么一般我们需要用一个Halo导管,一根可以弯折的上面带有很多对电极的导管,沿着折返环,环形放置。那么成功率也可以到95%。
1.在没有开始记录(空跑的状态下)和开始记录时的波形的基线都不在0点而是处于负值,是因为仪器设备设置的问题还是仪器本身有损坏?
2.记录ACC场电的通道50Hz干扰特别大,接地线排干扰后仍然存在,可能是什么问题呢?
3.Brownlee440的Amplifier上有Gain,lowpassfilter,Highpassfilter的设置,这个设置对ACC场电的记录有影响吗?如果记录ACC的场电,一般常用的参数是多少啊?
4.有没有用过这个仪器记录过肌电的前辈,我用A-B模式可以记录到类似Chart5软件记录的肌电波形。可是用clampfit10.2的Analyze--statistics--Measurement--Area分析,分析出来的数值太小,与波形不符。从波形看,明显有强的肌肉收缩,但是数值却没有明显差异。有前辈分析过肌电吗?是否我的分析方法不对?或者是应为问题1中提到的基线不在0点所引起的曲线下面积分析的误差?
感谢!
先来个简单介绍:
电生理检查在临床中的应用
(electrophysiologicalexamination)
一、脑电图
脑电图(EEG)检查:是在头部按一定部位放置8-16个电极,经脑电图机将脑细胞固有的生物电活动放大并连续描记在纸上的图形。正常情况下,脑电图有一定的规律性,当脑部尤其是皮层有病变时,规律性受到破坏,波形即发生变化,对其波形进行分析,可辅助临床对及脑部疾病进行诊断。
脑波按其频率分为:δ波(1-3c/s)θ波(4-7c/s)、α波(8-13c/s)、β波(14-25c/s)γ波(25c/s以上),δ和θ波称为慢波,β和γ波称为快波。依年龄不同其基本波的频率也不同,如3岁以下小儿以δ波为主,3-6岁以θ波为主,随年龄增长,α波逐渐增多,到成年人时以α波为主,但年龄之间无明确的严格界限,如有的儿童4、5岁枕部α波已很明显。正常成年人在清醒、安静、闭眼时,脑波的基本节律是枕部α波为主,其他部位则是以α波间有少量慢波为主。判断脑波是否正常,主要是根据其年龄,对脑波的频率、波幅、两侧的对称性以及慢波的数量、部位、出现方式及有无病理波等进行分析。许多脑部病变可引起脑波的异常。如颅内占位性病变(尤其是皮层部位者)可有限局性慢波;散发性脑炎,绝大部分脑电图呈现弥漫性高波幅慢波;此外如脑血管病、炎症、外伤、代谢性脑病等都有各种不同程度的异常,但脑深部和线部位的病变阳性率很低。须加指出的是,脑电图表现没有特异性,必须结合临床进行综合判断,然而对于癫痫则有决定性的诊断价值,在阗痫发作间歇期,脑电图可有阵发性高幅慢波、棘波、尖波、棘一慢波综合等所谓“痛性放电”表现。为了提高脑电图的阳性率,可依据不同的病变部位采用不同的电极放置方法。如鼻咽电极、鼓膜电极和蝶骨电极,在开颅时也可将电极置于皮层(皮层电极)或埋入脑深部结构(深部电极);此外,还可使用各种诱发试验,如睁闭眼、过度换气、闪光刺激、睡眠诱发、剥夺睡眠诱发以及静脉注射美解眠等。但蝶骨电极和美解眠诱发试验等方法,可给病人带来痛苦和损害,须在有经验者指导下进行。随着科技的日益发展,近年来又有了遥控脑电图和24小时监测脑电图。
二、脑电地形图(BEAM)
是在EEG的基础上,将脑电信号输入电脑内进行再处理,通过模数转换和付立叶转换,将脑电信号转换为数字信号,处理成为脑电功率谱,按照不同频带进行分类,依功率的多少分级,最终使脑电信号转换成一种能够定量的二维脑波图像,此种图象能客观地反映各部电位变化的空间分布状态,其定量标志可以用数字或颜色表示,再用打印机打印在颅脑模式图上,或贮存在软盘上。它的优越性在于能发现EEG中较难判别的细微异常,提高了阳性率,且病变部位图象直观醒目,定位比较准确,从而客观对大脑机能进行评价。主要应用于缺血性脑血管病的早期诊断及疗效予后的评价,小儿脑发育与脑波变化的研究,视觉功能的研究,大浮肿瘤的定位以及精神药物的研究等。
三、脑磁图
电流在导体内流动进,导体周围可以产生磁场。同理,脑细胞的电活动也有极微弱的磁场,可用高灵敏度的磁场传感器予以检测,并记录其随时间变化的关系曲线,是即脑磁图,其图形与EEG图形相似。与EEG相比,优点是:可发现有临床意义而又不能被EEG记录到的波形,或检测到皮质局限性的异常电磁活动;此外,磁检器不与头皮接触,也减少了干扰造成的伪差。若与EEG同时描记,还可对不同物理方位的皮质群进行分析。但由于屏蔽、电磁装置以及其他设备复杂、昂贵,目前国内尚无此项设备。
四、诱发电位
给人体感官、感觉神经或运动皮质、运动神经以刺激,兴奋沿相应的神经通路向中枢或外周传导,在传导过程中,产生的不断组合传递的电位变化,即为诱发电位,对其加以分析,即或反映出不同部位的神经功能状态。由于诱发电位非常微小,须借助电脑对重复刺激的信号进行叠加处理,将其放大,并从淹没于肌电、脑电的背景中提取出来,才能加以描记。主要是对波形、主波的潜伏期、波峰间期和波幅等进行分析,为临床诊断提供参考,目前临床常用的有视觉、脑干听觉、体感、运动和事件相关诱发电位,以及视网膜图和耳蜗电图等,可分别反映视网膜、视觉通路、内耳、听神经、脑干、外周神经、脊髓后索、感觉皮质以及上下运动神经元的各种病变,事件相关诱发电位则用以判断患者的注意力和反应能力。诱发电位具有高度敏感性,对感觉障碍可进行客观评诂,对病变能进行定量判断。对心理精神领域可进行一定的检测,故当前广泛应用于对神经系统病变的早期诊断,病情随访,疗效判断,予后估计,神经系统发育情况的评估以及协助判断昏迷性质和脑死亡等。但图形无特异性,必须结合临床资料进行判断;不在有关神经传导径路中的病变,不能发现异常。近年,诱发电位的频谱分析和诱发电位地形图也在临床上逐渐开始应用,进一步提高了其临床应用价值。
五、肌电图(EMG)
是用肌电图仪记录神经和肌肉的生物电活动,对其波形进行测量分析,可以了解神经、肌肉的功能状态,协助对下运动神经元或肌肉疾病的诊断。目前常用的方法有三种:①针极肌电图:亦称普通肌电图,是将特制的针电极刺入肌腹,或用表面电极置于肌肉表面皮肤,在示波器上或记录纸上观察肌肉在静止、轻收缩、重收缩三种状态下的电位变化,以帮助判断疾病究系神经源性或肌源性损害。②神经传导速度测定:也即运动神经传导速度(MCV)和感觉神经传导速度(SCV)测定。系在神经干的近端(MCV)或远端(SCV)给以脉冲刺激,在远端效应肌(MCV)或近端神经走行部位(SCV)接收波形,测理两点之间的潜伏期和距离,即可计算出运动神经或感觉神经传导速度,主要用于了解神经传导功能情况。③其他:如重复频率试验,F波、H反射、牵张反射等检查以及单纤维肌电图检查等,可进一步了解神经、肌肉、神经一肌接头以及脊髓反射弧的功能状态。
六、脑阻抗血流图(REG)
是检查头部血管功能和供血情况的一种方法。其原理是通过放置在头部的电极给以微弱的高频电流,由于血液的电阻率最小,其电阻可随心动周期供血的变化而变化,这种节律性的阻抗变化,经血流图仪放大,可描记出波动性曲线,对其进行测量、计算、分析,可间接了解外周阻力、血管弹性和供血情况。本法简便易行,但因影响因素比较多,如情绪、气温、检查当时的血管功能状态等,故对其判断应加慎重。须结合临床症状,体征等进行判断。常用于脑动脉硬化、闭塞性脑血管病、偏头痛以及药物疗效观察等。