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1
Purification and some properties of 1-aspartamido-beta-N-acetylglucosamine amidohydrolase from human liver.人肝脏中1-天冬氨酰-β-N-乙酰葡糖胺酰胺水解酶的纯化及某些性质
Biochem J. 1977 Sep 1;165(3):497-502. doi: 10.1042/bj1650497.
2
Effect of different compounds on 1-aspartamido-beta-N-acetylglucosamine amidohydrolase from human liver.不同化合物对人肝脏1-天冬酰胺-β-N-乙酰葡糖胺酰胺水解酶的影响。
Biochem J. 1978 Jun 1;171(3):799-802. doi: 10.1042/bj1710799.
3
Isolation of a human hepatic 60 kDa aspartylglucosaminidase consisting of three non-identical polypeptides.由三种不同多肽组成的人肝脏60 kDa天冬氨酰葡糖胺酶的分离
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4
Purification and properties of human hepatic aspartylglucosaminidase.人肝脏天冬氨酰葡糖胺酶的纯化及性质
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5
Measurement of 1-aspartamido-beta-N-acetylglucosamine amidohydrolase activity in human tissues.人体组织中1-天冬氨酰-β-N-乙酰葡糖胺酰胺水解酶活性的测定。
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6
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7
Distribution, purification and properties of 1-aspartamido-beta-N-acetylglucosamine amidohydrolase.1-天冬氨酰-β-N-乙酰葡糖胺酰胺水解酶的分布、纯化及性质
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Purification and structure of human liver aspartylglucosaminidase.人肝脏天冬氨酰葡糖胺酶的纯化与结构
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Drug Metab Dispos. 1981 Nov-Dec;9(6):573-7.

引用本文的文献

1
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J Inherit Metab Dis. 1982;5(4):197-203. doi: 10.1007/BF02179141.
2
Aspartylglycosaminuria: an inborn error of glycoprotein catabolism.天冬氨酰葡糖胺尿症:一种糖蛋白分解代谢的先天性缺陷。
J Inherit Metab Dis. 1982;5(4):192-6. doi: 10.1007/BF02179139.
3
Disturbed metabolism of copper and zinc in aspartylglycosaminuria: possible involvement with connective tissue changes.天冬氨酰葡糖胺尿症中铜和锌的代谢紊乱:可能与结缔组织变化有关。
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4
Absence of endo-beta-N-acetylglucosaminidase activity in the kidneys of sheep, cattle and pig.绵羊、牛和猪肾脏中缺乏内切-β-N-乙酰氨基葡萄糖苷酶活性。
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5
Isolation of a human hepatic 60 kDa aspartylglucosaminidase consisting of three non-identical polypeptides.由三种不同多肽组成的人肝脏60 kDa天冬氨酰葡糖胺酶的分离
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6
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7
Human leucocyte aspartylglucosaminidase. Evidence for two different subunits in a more complex native structure.人白细胞天冬氨酰葡糖胺酶。关于更复杂天然结构中两种不同亚基的证据。
Biochem J. 1991 May 15;276 ( Pt 1)(Pt 1):251-6. doi: 10.1042/bj2760251.
8
Spectrum of mutations in aspartylglucosaminuria.天冬氨酰葡糖胺尿症的突变谱
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9
Purification and structure of human liver aspartylglucosaminidase.人肝脏天冬氨酰葡糖胺酶的纯化与结构
Biochem J. 1992 Dec 15;288 ( Pt 3)(Pt 3):1005-10. doi: 10.1042/bj2881005.
10
Effect of different compounds on 1-aspartamido-beta-N-acetylglucosamine amidohydrolase from human liver.不同化合物对人肝脏1-天冬酰胺-β-N-乙酰葡糖胺酰胺水解酶的影响。
Biochem J. 1978 Jun 1;171(3):799-802. doi: 10.1042/bj1710799.

本文引用的文献

1
Protein measurement with the Folin phenol reagent.使用福林酚试剂进行蛋白质测定。
J Biol Chem. 1951 Nov;193(1):265-75.
2
BETA-(N-ACETYLGLUCOSAMINE)-N-GLYCOSIDASE: AN ENZYME WHICH CATALYZES THE HYDROLYSIS OF 1-BETA-ASPARTYL-2-ACETAMIDO-1,2-DIDEOXY-D-GLUCOSYLAMINE.β-(N-乙酰葡糖胺)-N-糖苷酶:一种催化1-β-天冬氨酰-2-乙酰氨基-1,2-二脱氧-D-葡糖胺水解的酶。
J Biol Chem. 1965 Jan;240:PC556-8.
3
Apparent co-operative effect of acetyl-CoA on pigeon liver pyruvate carboxylase.乙酰辅酶A对鸽肝丙酮酸羧化酶的明显协同效应。
FEBS Lett. 1973 Mar 1;30(2):181-184. doi: 10.1016/0014-5793(73)80647-7.
4
Beta-aspartylglucosylamine amido hydrolase of rat liver and kidney.大鼠肝脏和肾脏中的β-天冬氨酰葡糖胺酰胺水解酶
J Biol Chem. 1967 Oct 25;242(20):4568-76.
5
Enzymatic cleavage of glycopeptides.糖肽的酶促裂解
Biochem Biophys Res Commun. 1966 Sep 22;24(6):961-6. doi: 10.1016/0006-291x(66)90344-5.
6
Enzymatic cleavage of 2-acetamido-1-(beta'-L-aspartamido)-1,2-dideoxy-beta-D-glucose by human plasma and seminal fluid. Failure to detect the heterozygous state for aspartylglycosaminuria.人血浆和精液对2-乙酰氨基-1-(β'-L-天冬酰胺基)-1,2-二脱氧-β-D-葡萄糖的酶促裂解。未检测到天冬氨酰葡糖胺尿症的杂合状态。
Clin Chim Acta. 1969 Sep;25(3):413-6. doi: 10.1016/0009-8981(69)90201-0.
7
The purification and properties of a beta-aspartyl N-acetylglucosylamine amidohydrolase from hen oviduct.来自母鸡输卵管的β-天冬氨酰-N-乙酰葡糖胺酰胺水解酶的纯化及性质
Arch Biochem Biophys. 1969 Mar;130(1):295-303. doi: 10.1016/0003-9861(69)90036-8.
8
Studies on enzymes acting on glycopeptides.作用于糖肽的酶的研究。
J Biochem. 1968 Feb;63(2):186-92. doi: 10.1093/oxfordjournals.jbchem.a128760.
9
Distribution of a glycopeptide-degrading enzyme in tissue and cells.一种糖肽降解酶在组织和细胞中的分布。
Biochim Biophys Acta. 1968 Mar 11;156(2):417-9. doi: 10.1016/0304-4165(68)90276-6.
10
Distribution, purification and properties of 1-aspartamido-beta-N-acetylglucosamine amidohydrolase.1-天冬氨酰-β-N-乙酰葡糖胺酰胺水解酶的分布、纯化及性质
Biochem J. 1969 Dec;115(4):709-15. doi: 10.1042/bj1150709.

人肝脏中1-天冬氨酰-β-N-乙酰葡糖胺酰胺水解酶的纯化及某些性质

Purification and some properties of 1-aspartamido-beta-N-acetylglucosamine amidohydrolase from human liver.

作者信息

Dugal B, Stromme J

出版信息

Biochem J. 1977 Sep 1;165(3):497-502. doi: 10.1042/bj1650497.

DOI:10.1042/bj1650497
PMID:21658
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1164932/
Abstract

Human liver 1-aspartamido-beta-N-acetylglucosamine amidohydrolase (aspartylglucosylaminase, EC 3.5.1.26) was purified 17 500-fold to apparent homogeneity as judged from polyacrylamide-gel disc electrophoresis. A pH optimum of 7.7-9.0 was found. The Km value was pH- and temperature-dependent. At 37 degrees C and pH 7.7, Km was 0.16 mM and it increased to 0.29 at pH 6.0 and 0.23 at pH 9.0. At 25 degrees C and pH 7.7, a Km value of 0.99 mM was obtained. When the substrate concentration was varied, apparent Michaelis-Menten kinetics were obtained. p-Hydroxymercuribenzoate, glutathione or cysteine had no effect on the enzyme activity; 5 mM-N-acetylcysteine inhibited about 47% of the total enzyme activity. Apart from Cu2+, other bivalent ions were virtually ineffective at 1 mM. The kinetic study differentiates this enzyme from aspartylglucosylaminase from other sources.

摘要

人肝脏1-天冬氨酰-β-N-乙酰葡糖胺酰胺水解酶(天冬氨酰葡糖胺酶,EC 3.5.1.26)经纯化后,从聚丙烯酰胺凝胶圆盘电泳判断,其纯度提高了17500倍,达到了表观均一性。发现最适pH值为7.7 - 9.0。Km值受pH值和温度影响。在37℃和pH 7.7时,Km为0.16 mM,在pH 6.0时增加到0.29,在pH 9.0时为0.23。在25℃和pH 7.7时,Km值为0.99 mM。当底物浓度变化时,呈现出明显的米氏动力学。对羟基汞苯甲酸、谷胱甘肽或半胱氨酸对酶活性无影响;5 mM - N - 乙酰半胱氨酸抑制约47%的总酶活性。除Cu2+外,其他二价离子在1 mM时几乎无作用。动力学研究将该酶与其他来源的天冬氨酰葡糖胺酶区分开来。