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人脑苷脂硫酸酯酶激活剂。对无脊椎动物硫酸酯酶酸性形式的激活作用。

The activator of human cerebroside sulphatase. Activating effect on the acidic forms of the sulphatases from invertebrates.

作者信息

Mraz W, Fischer G, Jatzkewitz H

出版信息

Hoppe Seylers Z Physiol Chem. 1976 Feb;357(2):201-6. doi: 10.1515/bchm2.1976.357.1.201.

Abstract
  1. Acidic forms of the sulphatase were partially purified from the following invertebrate species: Tethya aurantium (Porifera), Patella vulgata (mollusca), Maja squinado (Arthropoda), Marthasterias glacialis (Echinodermata) and Microcosmus sulcatus (Tunicata). Enzyme preparations thus obtained cleaved cerebroside sulphates (sulphatides) only in the presence of either specific detergents (e.g. taurodeoxycholate) or an activator protein isolated from human liver. This corresponds to the findings on purified sulphatase A of human origin. 2) At low concentrations, the activating effect was proportional to the amount of activator protein applied; at higher concentrations, proportionality was obtained only in some cases. On a molar basis, less of the activator protein was required to achieve the same activation as taurodeoxycholate. At optimum concentrations of the detergent however, the activation was much higher. 3) The enzyme specificity of the activator and some evolutionary implications are discussed.
摘要
  1. 从以下无脊椎动物物种中部分纯化了硫酸酯酶的酸性形式:橙黄海绵(多孔动物门)、笠贝(软体动物门)、黄道蟹(节肢动物门)、冰川海星(棘皮动物门)和沟纹海鞘(被囊动物亚门)。由此获得的酶制剂仅在存在特定去污剂(如牛磺脱氧胆酸盐)或从人肝脏中分离出的激活蛋白时才能裂解脑苷脂硫酸盐(硫脂)。这与源自人类的纯化硫酸酯酶A的研究结果一致。2) 在低浓度下,激活作用与所施加的激活蛋白量成正比;在较高浓度下,仅在某些情况下才成正比。以摩尔为基础,与牛磺脱氧胆酸盐相比,实现相同激活所需的激活蛋白量更少。然而,在去污剂的最佳浓度下,激活作用要高得多。3) 讨论了激活剂的酶特异性和一些进化意义。

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The activator of cerebroside-sulphatase. A model of the activation.脑苷脂硫酸酯酶激活剂。激活模型。
Biochim Biophys Acta. 1978 Jan 27;528(1):69-76. doi: 10.1016/0005-2760(78)90053-x.
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Studies on the function of the activator of sulphatase A.硫酸酯酶 A 激活剂的功能研究。
Adv Exp Med Biol. 1978;101:573-82. doi: 10.1007/978-1-4615-9071-2_53.
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The activator of cerebroside sulphatase. Lysosomal localization.脑硫脂酶激活剂。溶酶体定位。
Hoppe Seylers Z Physiol Chem. 1976 Aug;357(8):1181-91. doi: 10.1515/bchm2.1976.357.2.1181.

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