胶原蛋白交联：鉴定软骨胶原蛋白中两个含有分子间交联形成位点的溴化氰肽段。 - Suppr

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超能文献

Collagen cross-linking: identification of two cyanogen bromide peptides containing sites of intermolecular cross-link formation in cartilage collagen.

作者信息

Miller E J

出版信息

Biochem Biophys Res Commun. 1971 Oct 15;45(2):444-51. doi: 10.1016/0006-291x(71)90839-4.

DOI:10.1016/0006-291x(71)90839-4

PMID:4334341

Abstract

摘要

相似文献

Collagen cross-linking: identification of two cyanogen bromide peptides containing sites of intermolecular cross-link formation in cartilage collagen.胶原蛋白交联：鉴定软骨胶原蛋白中两个含有分子间交联形成位点的溴化氰肽段。

Biochem Biophys Res Commun. 1971 Oct 15;45(2):444-51. doi: 10.1016/0006-291x(71)90839-4.

The stability of collagen cross-links when derived from hydroxylsyl residues.当源自羟赖氨酸残基时胶原蛋白交联的稳定性。

Biochem Biophys Res Commun. 1973 Sep 5;54(1):432-9. doi: 10.1016/0006-291x(73)90940-6.

Studies on the location of intermolecular cross-links in collagen. Isolation of a CNBr peptide containing -hydroxylysinonorleucine.胶原蛋白中分子间交联位置的研究。含γ-羟基赖氨酸正亮氨酸的溴化氰肽段的分离。

Biochemistry. 1972 May 9;11(10):1828-35. doi: 10.1021/bi00760a015.

Isolation of polypeptides containing the intermolecular cross-link , '-dihydroxylysinonorleucine from dentin collagen.从牙本质胶原蛋白中分离含有分子间交联物——γ-二羟基赖氨酰正亮氨酸的多肽。

Arch Biochem Biophys. 1973 Sep;158(1):106-15. doi: 10.1016/0003-9861(73)90602-4.

Structural studies on cartilage collagen employing limited cleavage and solubilization with pepsin.利用胃蛋白酶进行有限裂解和溶解对软骨胶原蛋白进行的结构研究。

Biochemistry. 1972 Dec 19;11(26):4903-9. doi: 10.1021/bi00776a005.

Isolation and characterization of the cyanogen bromide peptides from the alpha 1(II) chain of bovine and human cartilage collagen.从牛和人软骨胶原蛋白α1(II)链中分离并鉴定溴化氰肽段

Biochemistry. 1973 Aug 14;12(17):3153-9. doi: 10.1021/bi00741a003.

Collagen cross-linking. Isolation of cross-linked peptides from collagen of chicken bone.胶原蛋白交联。从鸡骨胶原蛋白中分离交联肽。

Biochem J. 1973 Nov;135(3):393-403. doi: 10.1042/bj1350393.

Cyanogen bromide peptides from insoluble skin and dentin bovine collagens.来自不溶性牛皮肤和牙本质胶原蛋白的溴化氰肽。

Biochemistry. 1973 Mar 27;12(7):1452-64. doi: 10.1021/bi00731a028.

Analysis of a crosslinked peptide from calf bone collagen: evidence that hydroxylysyl glycoside participates in the crosslink.小牛骨胶原蛋白交联肽的分析：羟赖氨酰糖苷参与交联的证据。

Biochem Biophys Res Commun. 1973 May 15;52(2):663-71. doi: 10.1016/0006-291x(73)90764-x.

The pyridoxal phosphate-binding site of rabbit muscle aldolase.兔肌肉醛缩酶的磷酸吡哆醛结合位点。

Arch Biochem Biophys. 1973 Jun;156(2):712-9. doi: 10.1016/0003-9861(73)90324-x.

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The response of foetal annulus fibrosus cells to growth factors: modulation of matrix synthesis by TGF-β1 and IGF-1.胎儿纤维环细胞对生长因子的反应：TGF-β1 和 IGF-1 对基质合成的调节。

Histochem Cell Biol. 2011 Aug;136(2):163-75. doi: 10.1007/s00418-011-0835-x. Epub 2011 Jul 8.

Identification of cyanogen bromide peptides involved in intermolecular cross-linking of bovine type III collagen.参与牛III型胶原分子间交联的溴化氰肽段的鉴定

Biochem J. 1980 Jan 1;185(1):195-201. doi: 10.1042/bj1850195.

Biochem J. 1974 May;139(2):461-8. doi: 10.1042/bj1390461.

Biochemistry of articular cartilage. Nature of proteoglycans and collagen of articular cartilage and their role in ageing and in osteoarthrosis.关节软骨的生物化学。关节软骨蛋白聚糖和胶原蛋白的性质及其在衰老和骨关节炎中的作用。

Ann Rheum Dis. 1973 Jul;32(4):364-78. doi: 10.1136/ard.32.4.364.

The chemistry of the collagen cross-links. The mechanism of stabilization of the reducible intermediate cross-links.胶原蛋白交联的化学性质。可还原中间交联的稳定机制。

Biochem J. 1975 Aug;149(2):381-5. doi: 10.1042/bj1490381.

Biochemical characteristics and biological significance of the genetically-distinct collagens.基因不同的胶原蛋白的生化特性及生物学意义。

Mol Cell Biochem. 1976 Dec 10;13(3):165-92. doi: 10.1007/BF01731779.

In vitro inhibition of chick embryo lysyl hydroxylase by homogentisic acid. A proposed connective tissue defect in alkaptonuria.尿黑酸对鸡胚赖氨酰羟化酶的体外抑制作用。对尿黑酸尿症中一种推测的结缔组织缺陷的研究。

J Clin Invest. 1977 Jun;59(6):1071-9. doi: 10.1172/JCI108730.

Biochemical and physiochemical characterization of pepsin-solubilized type-II collagen from bovine articular cartilage.牛关节软骨中胃蛋白酶溶解的II型胶原蛋白的生化和物理化学特性

Biochem J. 1977 Feb 1;161(2):303-12. doi: 10.1042/bj1610303.

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