藥物濫用（MOR）多合一聯(lián)檢試劑

藥物濫用（MOR）多合一聯(lián)檢試劑

廣州健侖生物科技有限公司

我司同時(shí)有bzo - bar - coc - thc met - - opi - oxy - mdma - cfp - amp - xtc – bat多聯(lián)檢測(cè)卡（膠體金法）

主營(yíng)品牌：美國(guó)NovaBios、美國(guó)Cortez、國(guó)產(chǎn)創(chuàng)侖等等。

主要用途：篩查違禁品濫用殘留、麻醉藥殘留、興奮藥物殘留等等。

反應(yīng)快違禁品檢測(cè)試紙

反應(yīng)快違禁品檢測(cè)試紙

檢測(cè)范圍：嗎啡、KET、mamp、MDMA、BZO、THC、巴比妥、MTD、BAR、MDMA、AMP、BUP、PCP、TCA、OXY、MET等等。

藥物濫用（MOR）多合一聯(lián)檢試劑

產(chǎn)品特點(diǎn)：可以根據(jù)需求自主訂制多聯(lián)卡。多聯(lián)卡自由組合，從二聯(lián)到十五聯(lián)都可以訂制。

我司還提供其它進(jìn)口或國(guó)產(chǎn)試劑盒：登革熱、瘧疾、流感、A鏈球菌、合胞病毒、腮病毒、乙腦、寨卡、黃熱病、基孔肯雅熱、克錐蟲病、違禁品濫用、肺炎球菌、軍團(tuán)菌、化妝品檢測(cè)、食品安全檢測(cè)等試劑盒以及日本生研細(xì)菌分型診斷血清、德國(guó)SiFin診斷血清、丹麥SSI診斷血清等產(chǎn)品。

如需訂購(gòu)或者了解請(qǐng)以下或

mob： 楊   ： 

NTERPRETATION OF RESULTS

更多產(chǎn)品說明可通過下方的進(jìn)行了解

添加掃一掃二維碼：

【公司名稱】 廣州健侖生物科技有限公司

【 市場(chǎng)部 】       楊永漢
【】 
【騰訊  】
【公司地址】 廣州市清華科技園健新基地番禺石樓鎮(zhèn)健啟路63號(hào)二期2幢101-103室

高等動(dòng)物的細(xì)胞色素c由個(gè)氨基酸殘基的一條肽鏈組成；分子 量約為,在共價(jià)結(jié)合的血紅素輔基中；鐵原子的第、個(gè)配位鍵被組氨酸咪唑 基的氮原子和甲硫氨酸的硫原子所占據(jù),因而還原型的細(xì)胞色素c不 能被氧直接氧化。它催化電子從細(xì)胞色素還原酶（或稱bc復(fù)合物 ） 傳遞到細(xì)胞色素氧化酶（或稱細(xì)胞色素）。已對(duì)多種不 同種屬的細(xì)胞色素c進(jìn)行了一級(jí)結(jié)構(gòu)測(cè)定，并根據(jù)其氨基酸變異數(shù) 繪制了種屬發(fā)生圖，這不僅揭示了細(xì)胞色素c在進(jìn)化上來自一個(gè)共 同的祖先,也可以據(jù)此估計(jì)生物的主要種屬發(fā)生進(jìn)化的可能時(shí)間。 細(xì)胞色素b和c是輔酶Q-細(xì)胞色素c還原體系中的兩個(gè)帶氧化還原 中心的組分。細(xì)胞色素b是一個(gè)橫貫?zāi)蓚?cè)的疏水性的蛋白。 對(duì)細(xì)胞色素b氨基酸組成和結(jié)構(gòu)基因的脫氧核糖核酸(DN)順序研 究指出,約%的氨基酸為非極性的。對(duì)細(xì)胞色素b在電子傳遞鏈中 的復(fù)雜功能至今還不清楚。細(xì)胞色素c的多肽由一個(gè)大的親水部分 和一個(gè)小的疏水部分組成，親水區(qū)帶有血紅素輔基伸出在膜外的水 相中，與細(xì)胞色素c有一個(gè)結(jié)合點(diǎn)。
The cytochrome c in higher animals consists of one peptide chain of amino acid residues; the molecular weight is about that in the covalently bonded hemophile auxiliary group; the first and the second coordinate bond of the iron atom is the histidine imidazole group nitrogen atom. It is occupied by sulfur atoms of methionine, so that reduced cytochrome c cannot be directly oxidized by oxygen. It catalyzes the transfer of electrons from the cytochrome reductase (or bc complex) to cytochrome oxidase (or cytochrome). The primary structure of cytochrome c has been determined for a variety of different species, and species-specific maps have been mapped based on amino acid variations. This not only reveals that cytochrome c has evolved from a common ancestor, but also This estimate of the likely time of evolution of the main species of the organism. Cytochromes b and c are two redox-centered components in the coenzyme Q-cytochrome c reduction system. Cytochrome b is an extremely hydrophobic protein that traverses both sides of the membrane. The deoxyribonucleic acid (DN) sequence studies of cytochrome b amino acid composition and structural genes indicate that about % of amino acids are non-polar. The complex function of cytochrome b in the electron transport chain is still unknown. The polypeptide of cytochrome c consists of a large hydrophilic portion and a small hydrophobic portion. The hydrophilic region carries the heme prosthetic group out of the aqueous membrane and has a binding site with cytochrome c.