Comparison of liver glycosylasparaginases from six vertebrates.

Comparison of liver glycosylasparaginases from six vertebrates.
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六种脊椎动物肝脏糖基门冬酰胺酶的比较。

DOI:
10.1042/bj2820891
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发表时间:
1992
期刊:
The Biochemical journal
影响因子:
--
通讯作者:
AronsonJr,NN
AronsonJr,NN
中科院分区:
--
文献类型:
--
作者:
Tollersrud,OK;AronsonJr,NN

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比较了人、猪、牛、大鼠、小鼠和鸡肝中糖基天冬酰胺酶(EC 3.5.1.26)的结构和物理性质。所有物种中的酶具有通过非共价力连接的约24(α)和20(β)kDa的两个N-糖基化亚基的共同基本结构。针对大鼠糖基天冬酰胺酶的亚单位特异性抗血清特异性和敏感性结合到所有物种的相应亚单位。在相应的猪和大鼠糖基天冬酰胺酶α-和β-亚基的N-末端序列与来自人糖基天冬酰胺酶cDNA的推导序列之间发现80%的氨基酸的同一性[Fisher,Tollersrud & Aronson(1990)FEBS Lett. 269,440-444]。来自所有三个物种的β-亚基具有N-末端苏氨酸,据报道其参与人酶的反应机制[Kaartinen,威廉姆斯,Tomich,Yates,Hood & Mononen(1991)J. Biol. Chem. 266,5860-5869]。天然酶在哺乳动物中表现为异二聚体,而鸡酶具有更大的分子量,并且可能是与不相关肽结合的四聚体或异二聚体。所有糖基天冬酰胺酶都是热稳定的,需要65摄氏度到80摄氏度之间的温度才能不可逆地失活。此外,它们在高pH值下异常稳定,在SDS存在下保持活性,但在低pH值下除外。最大pH值介于5.5和6之间,但大鼠和小鼠酶在pH值7和8之间具有广泛的最大值。还观察到许多其他性质,这些性质也将该酶与个体和密切相关的物种区分开来。
Structural and physical properties of glycosylasparaginase (EC 3.5.1.26) from the livers of human, pig, cow, rat, mouse and chicken were compared. The enzyme in all species had a common basic structure of two N-glycosylated subunits of about 24 (alpha) and 20 (beta) kDa joined by non-covalent forces. Subunit-specific antisera against the rat glycosylasparaginase bound specifically and sensitively to the corresponding subunits from all species. Identity of 80% of the amino acids was found between the N-terminal sequences of corresponding pig and rat glycosylasparaginase alpha- and beta-subunits and the deduced sequence from a human glycosylasparaginase cDNA [Fisher, Tollersrud & Aronson (1990) FEBS Lett. 269, 440-444]. The beta-subunit from all three species has an N-terminal threonine reported to be involved in the reaction mechanism for the human enzyme [Kaartinen, Williams, Tomich, Yates, Hood & Mononen (1991) J. Biol. Chem. 266, 5860-5869]. The native enzyme appeared as a heterodimer among the mammals, whereas the chicken enzyme had a greater molecular mass and is probably either a tetramer or a heterodimer bound to an unrelated peptide(s). All glycosylasparaginases were thermostable, requiring temperatures between 65 degrees C and 80 degrees C to be irreversibly inactivated. In addition, they were unusually stable at high pH and remained active in the presence of SDS except at low pH. The pH maximum was between 5.5 and 6 except for the rat and mouse enzymes which had a broad maximum between pH 7 and 8. A number of other properties were observed which also distinguish the enzyme from individual and closely related species.
人类精子的运动特征与其穿透宫颈粘液和无带仓鼠卵母细胞的能力之间的关系。
DOI: 10.1530/jrf.0.0730441
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影响因子: --
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发表时间: 1985
影响因子: 6.7
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影响因子: 6.7
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影响因子: --
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DOI: 10.1016/0169-2607(85)90002-1
发表时间: 1985
影响因子: 6.1
作者:
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通讯作者: James W. Overstreet