Aspartate aminotransferase immobilized on collagen films. Activity of dissociated subunits.
作者信息
Arrio-Dupont M, Coulet P R
出版信息
Biochem Biophys Res Commun. 1979 Jul 27;89(2):345-52. doi: 10.1016/0006-291x(79)90636-3.
PMID:486166
Abstract
摘要
相似文献
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Aspartate aminotransferase immobilized on collagen films. Activity of dissociated subunits.固定在胶原膜上的天冬氨酸转氨酶。解离亚基的活性。
Biochem Biophys Res Commun. 1979 Jul 27;89(2):345-52. doi: 10.1016/0006-291x(79)90636-3.
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Coupled reaction of immobilized aspartate aminotransferase and malate dehydrogenase. A plausible model for the cellular behaviour of these enzymes.固定化天冬氨酸转氨酶与苹果酸脱氢酶的偶联反应。这些酶细胞行为的一种合理模型。
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Immobilization of aspartate aminotransferase on agarose.
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Cytosolic aspartate aminotransferase. Studies on subunit interactions with the apo/holo hybrid dimer.胞质天冬氨酸转氨酶。亚基与脱辅基/全酶杂交二聚体相互作用的研究。
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Catalytic function of a histidyl residue in cytosolic aspartate aminotransferase-catalyzed reactions.胞质天冬氨酸转氨酶催化反应中组氨酸残基的催化功能。
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Phosphopyridoxyl peptide from chicken heart aspartate aminotransferase.来自鸡心脏天冬氨酸转氨酶的磷酸吡哆醛肽。
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Limited proteolytic cleavage of aspartate aminotransferase isoenzymes.天冬氨酸转氨酶同工酶的有限蛋白水解切割
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Interactions between aspartate animotransferase protomers observed during holoenzyme reconstitution.全酶重构过程中观察到的天冬氨酸氨基转移酶亚基间的相互作用。
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NMR studies of 6-fluoropyridoxal 5'-phosphate-containing cytosolic aspartate aminotransferase.含6-氟吡哆醛5'-磷酸的胞质天冬氨酸氨基转移酶的核磁共振研究
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引用本文的文献
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Three-dimensional structure of a pyridoxal-phosphate-dependent enzyme, mitochondrial aspartate aminotransferase.一种磷酸吡哆醛依赖性酶——线粒体天冬氨酸氨基转移酶的三维结构
Proc Natl Acad Sci U S A. 1980 May;77(5):2559-63. doi: 10.1073/pnas.77.5.2559.
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Subunit interactions in tyrosinase from frog epidermis in immobilized enzyme systems.固定化酶系统中青蛙表皮酪氨酸酶的亚基相互作用
Biochem J. 1981 Sep 1;197(3):581-9. doi: 10.1042/bj1970581.
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Shared active sites in oligomeric enzymes: model studies with defective mutants of aspartate transcarbamoylase produced by site-directed mutagenesis.寡聚酶中的共享活性位点：定点诱变产生的天冬氨酸转氨甲酰酶缺陷突变体的模型研究
Proc Natl Acad Sci U S A. 1987 Jan;84(1):31-5. doi: 10.1073/pnas.84.1.31.
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