（14C）原胶原的纯化及其脯氨酰羟化酶的羟化作用 - Suppr

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Purification of (14C) protocollagen and its hydroxylation by prolyl-hydroxylase.

作者信息

Berg R A, Prockop D J

出版信息

Biochemistry. 1973 Aug 28;12(18):3395-401. doi: 10.1021/bi00742a005.

DOI:10.1021/bi00742a005

PMID:4354367

Abstract

摘要

相似文献

Purification of (14C) protocollagen and its hydroxylation by prolyl-hydroxylase.（14C）原胶原的纯化及其脯氨酰羟化酶的羟化作用

Biochemistry. 1973 Aug 28;12(18):3395-401. doi: 10.1021/bi00742a005.

Intracellular collagen and protocollagen from embryonic tendon cells.来自胚胎肌腱细胞的细胞内胶原蛋白和前胶原蛋白。

J Biol Chem. 1973 Jan 25;248(2):720-9.

Concomitant hydroxylation of proline and lysine residues in collagen using purified enzymes in vitro.在体外使用纯化酶对胶原蛋白中的脯氨酸和赖氨酸残基进行伴随羟基化。

Biochim Biophys Acta. 1984 Jul 16;800(1):59-65. doi: 10.1016/0304-4165(84)90094-1.

Intracellular hydroxylation of non-helical protocollagen to form triple-helical procollagen and subsequent secretion of the molecule.非螺旋原胶原蛋白的细胞内羟基化以形成三螺旋前胶原蛋白，随后该分子被分泌。

Eur J Biochem. 1974 Apr 1;43(2):221-30. doi: 10.1111/j.1432-1033.1974.tb03403.x.

Effects of temperature on conformation, hydroxylation, and secretion of chick tendon procollagen.温度对鸡肌腱原胶原的构象、羟基化及分泌的影响

J Biol Chem. 1974 Jul 25;249(14):4480-6.

Hydroxylation of lysyl residues in native and denatured protocollagen by protocollagen lysyl hydroxylase in vitro.原胶原赖氨酰羟化酶在体外对天然和变性原胶原中赖氨酰残基的羟化作用。

Biochim Biophys Acta. 1974 Mar 20;343(1):129-37. doi: 10.1016/0304-4165(74)90244-x.

Hydroxyproline content determines the denaturation temperature of chick tendon collagen.羟脯氨酸含量决定鸡肌腱胶原蛋白的变性温度。

Arch Biochem Biophys. 1973 Oct;158(2):478-84. doi: 10.1016/0003-9861(73)90539-0.

Affinity column purification of protocollagen proline hydroxylase from chick embryos and further characterization of the enzyme.从鸡胚中亲和柱纯化原胶原脯氨酸羟化酶并对该酶进行进一步表征。

J Biol Chem. 1973 Feb 25;248(4):1175-82.

Labeled antibodies to protocollagen proline hydroxylase from chick embryos for intracellular localization of the enzyme.用于鸡胚原胶原蛋白脯氨酸羟化酶细胞内定位的标记抗体。

Biochim Biophys Acta. 1972 Nov 28;285(1):167-75. doi: 10.1016/0005-2795(72)90188-2.

Collagen biosynthesis.胶原蛋白生物合成

CRC Crit Rev Biochem. 1975 Feb;2(4):417-53. doi: 10.3109/10409237509102549.

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Bacillus anthracis Prolyl 4-Hydroxylase Modifies Collagen-like Substrates in Asymmetric Patterns.炭疽芽孢杆菌脯氨酰4-羟化酶以不对称模式修饰类胶原蛋白底物。

J Biol Chem. 2016 Jun 17;291(25):13360-74. doi: 10.1074/jbc.M116.725432. Epub 2016 Apr 21.

Prolyl 4-hydroxylase.脯氨酰4-羟化酶

Crit Rev Biochem Mol Biol. 2010 Apr;45(2):106-24. doi: 10.3109/10409231003627991.

Type I collagen in Hsp47-null cells is aggregated in endoplasmic reticulum and deficient in N-propeptide processing and fibrillogenesis.热休克蛋白47基因缺失细胞中的I型胶原蛋白在内质网中聚集，在N端前肽加工和原纤维形成方面存在缺陷。

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Production of recombinant human type I procollagen homotrimer in the mammary gland of transgenic mice.在转基因小鼠乳腺中生产重组人I型原胶原同三聚体。

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Catalytic properties of lysyl hydroxylase from cells synthesizing genetically different collagen types.合成基因不同类型胶原蛋白的细胞中赖氨酰羟化酶的催化特性。

Biochem J. 1982 Jan 1;201(1):215-9. doi: 10.1042/bj2010215.

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