鹵化酶 的英文怎麼說
中文拼音 [lǔhuà]
鹵化酶
英文
halidase-
The hatching enzyme from brine shrimp, artemia shrimp, is a pivotal protease which help the encysted embryo escape from its hatching membrane when hatching
鹵蟲孵化酶( he )是由鹵蟲早期胚胎特異性分泌的、在孵化過程中起關鍵作用的一種蛋白酶。The he was strongly inhibited by sbti and apmsf, and very sensitive to pmsf, lbti, and tlck, while not sensitive to chymostatin, bestatin, leupeptin, tpck, pepstatin, nem and iam. all these results imply that brine shrimp he was most probably a trypsin - type serine protease. the he could be strongly inhibited by edta in a dose - dependent manner, and 50 mmol / l edta exhibited more than 56. 5 % inhibition
對孵化酶純化樣品進行生化性質和酶性質分析發現,鹵蟲孵化酶的最適反應溫度約為40 ,最適ph為8 . 5左右;該孵化酶對p - apmsf 、 sbti極為敏感,對pmsf 、 lbti和tlck也非常敏感,但對chymostatin 、 leupeptin 、 pepstatin 、 bestatin 、 tpck 、 nem和iam不敏感,表明該酶極可能是一種屬于胰蛋白酶類型的絲氨酸蛋白酶。The distribution of the brine shrimp hgcs varies greatly from the species studied till now. one hour after hatching, neither the dorsal - anterior area nor the other dorsal area remained positive immunoreactivity signal. and 2 hours after hatching, there was no typical hgcs in the body of the brine shrimp and the remained hatching enzymes may participate in digesting the left vitellin in the nauplius
鹵蟲hgc最初出現至孵化前1h時均為全身性分佈,從孵出到孵出后2h ,頭鹵蟲孵化酶的生物化學性質及孵化腺細胞的免疫組織化學研究部的孵化酶顆粒已經減少,而變為非全身性分佈,到孵出后sh ,孵化酶顆粒已基本消失殆盡。Potent intracellular bactericidal action may be exerted through the myeloperoxidase-hydrogen peroxide-halide bactericidal system.
強烈的胞內殺菌作用可以通過骨髓過氧化物酶-過氧化氫-鹵素殺菌系統發揮威力。From the above results it can be concluded that the dorsal - anterior area and the dorsal area are probably the main position of he secretion
孵出后仍殘留的孵化酶有可能參與了鹵蟲幼體內殘余卵黃顆粒的消化降解,此結論還需進一步驗證。The brine shrimp he was prepared and purified by 67 % ammonium sulfate precipitation, deae - sepharose fast flow ion - exchange chromatography, and sephacryl column gel - filtration, and its biochemical and enzymological properties were identified in this study. it was found that the deduced molecular weight of he in sds - page is about 98. 5 kda, and its proteolytic activity was optimized at ph of 7. 5 - 8. 5 and at temperature of 40, respectively
我們利用67硫酸銨沉澱、 deae - sepharosefastflow陰離子交換柱層析和sephacryl凝膠過濾柱層析,並以酪蛋白為其蛋白酶水解活性的檢測底物、以卵膜為其卵殼裂解活性的特異性底物,從鹵蟲胚胎孵化液中分離純化出了鹵蟲的孵化酶分子,其在sds - page電泳中的分子量約為98 . 5kda 。分享友人