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白蛋白对二氢睾酮具有内在的烯醇化酶活性,这可以区分良性和恶性乳腺肿瘤。

Albumin possesses intrinsic enolase activity towards dihydrotestosterone which can differentiate benign from malignant breast tumors.

作者信息

Drmanovic Z, Voyatzi S, Kouretas D, Sahpazidou D, Papageorgiou A, Antonoglou O

机构信息

Theagenion Cancer Hospital, Thessaloniki, Greece.

出版信息

Anticancer Res. 1999 Sep-Oct;19(5B):4113-24.

Abstract

Serum albumin was found to possess enolase activity towards the dihydrotestesterone (DHT) molecule, converting it from its 3-keto to 3-enol form. This activity was accompanied by albumin during all stages of purification, as well as following various treatments, a fact indicating that the enzymatic activity was an intrinsic property of albumin molecule and did not represent an impurity of the preparation. Enolase activity was decreased in parallel with the quantity of intact albumin molecules when proteolytic enzymes were used for their degradation. The activity was strongly inhibited by Ni (II) and Cu (II) ions, which bind to 3-histidine of the albumin molecule, as well as by oleic acid and cholesterol. It was also inhibited, in a reversible manner by surface-active agents. Enolase activity was found in all mammalian species studied, the specific activity however was very low in the serum of dogs. The administration of DHT to mice did not influence the albumin or enolase levels in their serum. The optimum pH of enolase was at 9.2, with a carbonate buffer solution. In addition to the serum enolase activity was found to be a feature of intracellular albumin. The two albumins exhibited the same specific activity and the same Km for DHT. The study of cytosolic albumin, obtained from human mammary gland tissue, revealed that benign and malignant tumors of this gland differed substantially with respect to their percentage of albumin. Significant differences were also observed in enolase activity, a consequence of the existence of a fraction of albumin in the malignant tissue in a polymeric form. This form exhibited a decreased enzymatic activity, compared to its monomeric form, exclusively encountered in benign breast specimens. The last observation, along with the quantitative differences of albumin in the two tissues, offers a possibility of reliable differentiation between benign and malignant breast tumors.

摘要

血清白蛋白被发现对双氢睾酮(DHT)分子具有烯醇化酶活性,可将其从3 - 酮形式转化为3 - 烯醇形式。在纯化的各个阶段以及经过各种处理后,这种活性都与白蛋白相伴,这一事实表明该酶活性是白蛋白分子的固有特性,并非制剂的杂质。当使用蛋白水解酶降解时,烯醇化酶活性与完整白蛋白分子的数量平行下降。该活性受到与白蛋白分子的3 - 组氨酸结合的镍(II)和铜(II)离子、油酸和胆固醇的强烈抑制。它也受到表面活性剂的可逆抑制。在所研究的所有哺乳动物物种中都发现了烯醇化酶活性,然而狗血清中的比活性非常低。给小鼠注射DHT并不影响其血清中的白蛋白或烯醇化酶水平。烯醇化酶的最适pH值在9.2,使用碳酸盐缓冲溶液。除了血清烯醇化酶活性外,还发现其是细胞内白蛋白的一个特征。这两种白蛋白对DHT表现出相同的比活性和相同的Km值。对从人乳腺组织获得的细胞溶质白蛋白的研究表明,该腺体的良性和恶性肿瘤在白蛋白百分比方面有很大差异。在烯醇化酶活性方面也观察到显著差异,这是由于恶性组织中存在一部分聚合形式的白蛋白。与仅在良性乳腺标本中出现的单体形式相比,这种形式的酶活性降低。最后这一观察结果,连同两种组织中白蛋白的定量差异,为可靠区分良性和恶性乳腺肿瘤提供了可能性。

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