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Ultrastructural localization of pyruvate dehydrogenase in rat heart muscle.

作者信息

Nestorescu M L, Siess E A, Wieland O H

出版信息

Histochemie. 1973 Mar 26;34(4):355-60. doi: 10.1007/BF00306307.

DOI:10.1007/BF00306307
PMID:4697786
Abstract
摘要

相似文献

1
Ultrastructural localization of pyruvate dehydrogenase in rat heart muscle.大鼠心肌中丙酮酸脱氢酶的超微结构定位
Histochemie. 1973 Mar 26;34(4):355-60. doi: 10.1007/BF00306307.
2
Stimulation by calcium ions of pyruvate dehydrogenase phosphate phosphatase.钙离子对丙酮酸脱氢酶磷酸磷酸酶的刺激作用。
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[Studies on pig heart 2-oxoglutarate dehydrogenase (author's transl)].猪心脏2-氧代戊二酸脱氢酶的研究（作者译）
Seikagaku. 1974 Jul 25;46(7):325-35.
4
[Effect of ethanol on pyruvate catabolism in the rat].[乙醇对大鼠丙酮酸分解代谢的影响]
Z Ernahrungswiss. 1973 Mar;12(1):41-9. doi: 10.1007/BF02021944.
5
Multiplicity and origin of isoenzymes of lipoyl dehydrogenase.硫辛酰脱氢酶同工酶的多样性与起源
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6
Regulation of pyruvate dehydrogenase in rat heart. Mechanism of regulation of proportions of dephosphorylated and phosphorylated enzyme by oxidation of fatty acids and ketone bodies and of effects of diabetes: role of coenzyme A, acetyl-coenzyme A and reduced and oxidized nicotinamide-adenine dinucleotide.大鼠心脏中丙酮酸脱氢酶的调节。脂肪酸和酮体氧化对去磷酸化和磷酸化酶比例的调节机制以及糖尿病的影响：辅酶A、乙酰辅酶A以及还原型和氧化型烟酰胺腺嘌呤二核苷酸的作用
Biochem J. 1976 Feb 15;154(2):327-48. doi: 10.1042/bj1540327.
7
[Demonstration of pyruvate dehydrogenase complexes from swine heart mitochondria].[猪心脏线粒体丙酮酸脱氢酶复合物的展示]
Hoppe Seylers Z Physiol Chem. 1969 Oct;350(10):1161.
8
-Keto acid dehydrogenase complexes. XVII. Kinetic and regulatory properties of pyruvate dehydrogenase kinase and pyruvate dehydrogenase phosphatase from bovine kidney and heart.-酮酸脱氢酶复合体。十七。牛肾和心脏中丙酮酸脱氢酶激酶和丙酮酸脱氢酶磷酸酶的动力学及调节特性
Arch Biochem Biophys. 1972 Jul;151(1):328-40. doi: 10.1016/0003-9861(72)90504-8.
9
Ultrastructural localization of glutamic oxalacetic transaminase activity in cardiac muscle fiber and cardiac mitochondrial fraction of the rat.大鼠心肌纤维和心脏线粒体组分中谷氨酸草酰乙酸转氨酶活性的超微结构定位
Histochemie. 1969;19(2):99-109. doi: 10.1007/BF00281089.
10
Inframicroscopical localization of lipoic dehydrogenase.硫辛酸脱氢酶的亚显微镜定位
Acta Histochem. 1969;32(1):187-92.

引用本文的文献

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Novel O-palmitolylated beta-E1 subunit of pyruvate dehydrogenase is phosphorylated during ischemia/reperfusion injury.新型 O-软脂酰化丙酮酸脱氢酶 E1 亚基在缺血/再灌注损伤期间发生磷酸化。
Proteome Sci. 2010 Jul 9;8:38. doi: 10.1186/1477-5956-8-38.

本文引用的文献

1
The use of lead citrate at high pH as an electron-opaque stain in electron microscopy.在电子显微镜检查中，将高pH值的柠檬酸铅用作电子不透明染色剂。
J Cell Biol. 1963 Apr;17(1):208-12. doi: 10.1083/jcb.17.1.208.
2
Improvements in epoxy resin embedding methods.环氧树脂包埋方法的改进。
J Biophys Biochem Cytol. 1961 Feb;9(2):409-14. doi: 10.1083/jcb.9.2.409.
3
The membrane systems of the mitochondrion. II. The K fraction of the outer membrane of beef heart mitochondria.线粒体的膜系统。II. 牛心线粒体外膜的K组分
Arch Biochem Biophys. 1966 Jul;115(1):165-71. doi: 10.1016/s0003-9861(66)81052-4.
4
The use of ferricyanide for the light and electron microscopic demonstration of succinic dehydrogenase activity.用铁氰化物进行琥珀酸脱氢酶活性的光镜和电镜显示
Histochemie. 1968;14(4):343-51. doi: 10.1007/BF00304258.
5
Enzymatic properties of the inner and outer membranes of rat liver mitochondria.大鼠肝脏线粒体内膜和外膜的酶学特性
J Cell Biol. 1968 Jul;38(1):158-75. doi: 10.1083/jcb.38.1.158.
6
Interconversion and kinetic properties of pyruvate dehydrogenase from brain.大脑丙酮酸脱氢酶的相互转化及动力学特性
Hoppe Seylers Z Physiol Chem. 1971 Mar;352(3):447-52. doi: 10.1515/bchm2.1971.352.1.447.
7
Ultrastructural localization of succinate dehydrogenase in mouse liver mitochondria; a cytochemical study.小鼠肝脏线粒体中琥珀酸脱氢酶的超微结构定位；一项细胞化学研究。
J Histochem Cytochem. 1971 Feb;19(2):124-30. doi: 10.1177/19.2.124.
8
Inframicroscopical localization of lipoic dehydrogenase.硫辛酸脱氢酶的亚显微镜定位
Acta Histochem. 1969;32(1):187-92.
9
Enzyme localization in beef-heart mitochondria. A biochemical and electron-microscopic study.牛肉心线粒体中的酶定位：一项生物化学与电子显微镜研究
Eur J Biochem. 1972 Aug 18;29(1):47-59. doi: 10.1111/j.1432-1033.1972.tb01955.x.
10
[Structure of pyruvate dehydrogenase complex of pig heart muscle].[猪心肌丙酮酸脱氢酶复合体的结构]
Biochim Biophys Acta. 1971 Dec 15;250(3):478-90. doi: 10.1016/0005-2744(71)90248-8.