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纯化鸡凝集素的鸡组织结合位点

Chicken tissue binding sites for a purified chicken lectin.

作者信息

Beyer E C, Barondes S H

出版信息

J Supramol Struct. 1980;13(2):219-27. doi: 10.1002/jss.400130210.

DOI:10.1002/jss.400130210
PMID:7017279
Abstract

A lactose-binding lectin previously purified from embryonic chicken muscle and adult chicken liver, and here referred to as chicken-lactose-lectin-I (CLL-I), was added to sections of various adult chicken tissues to detect available binding sites. Both the sites of binding of added CLL-I as well as the tissue distribution of endogenous CLL-I were determined by indirect immunofluorescence using a rabbit antibody to CLL-I followed by fluorescent goat anti-rabbit IgG. Some tissues such as intestine and kidney showed abundant extracellular binding sites for the lectin, primarily between cells, in basement membrane, and in material on the luminal surface. In contrast, adult heart showed no significant binding sites for CLL-I. Adult pancreas showed considerable endogenous CLL-I in an extracellular site surrounding exocrine lobules, but added CLL-I did not bind substantially. The distribution of CLL-I binding sites in intestine were mimicked by those of purpurin, another lactose-binding lectin. CLL-I binding sites were also detected on the surface of cultured chick embryo skin fibroblasts. The factors controlling the specific distribution of occupied and unoccupied CLL-I binding sites are not known.

摘要

一种先前从胚胎鸡肌肉和成年鸡肝脏中纯化出来的乳糖结合凝集素,在此称为鸡乳糖凝集素-I(CLL-I),被添加到各种成年鸡组织切片中以检测可用的结合位点。通过使用抗CLL-I的兔抗体,随后用荧光山羊抗兔IgG进行间接免疫荧光,确定添加的CLL-I的结合位点以及内源性CLL-I的组织分布。一些组织,如肠道和肾脏,显示出该凝集素丰富的细胞外结合位点,主要在细胞之间、基底膜以及腔表面的物质中。相比之下,成年心脏未显示出CLL-I显著的结合位点。成年胰腺在外分泌小叶周围的细胞外位点显示出相当数量的内源性CLL-I,但添加的CLL-I并未大量结合。肠道中CLL-I结合位点的分布与另一种乳糖结合凝集素紫红素的分布相似。在培养的鸡胚皮肤成纤维细胞表面也检测到了CLL-I结合位点。控制占据和未占据的CLL-I结合位点特定分布的因素尚不清楚。

相似文献

1
Chicken tissue binding sites for a purified chicken lectin.纯化鸡凝集素的鸡组织结合位点
J Supramol Struct. 1980;13(2):219-27. doi: 10.1002/jss.400130210.
2
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Endogenous lectins in chickens and slime molds: transfer from intracellular to extracellular sites.鸡和黏菌中的内源性凝集素:从细胞内位点转移至细胞外位点。
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Two lactose binding lectins from chicken tissues. Purified lectin from intestine is different from those in liver and muscle.来自鸡组织的两种乳糖结合凝集素。从肠道中纯化的凝集素与肝脏和肌肉中的凝集素不同。
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Isolation and characterization of a soluble lactose-binding lectin from postnatal chicken retina.产后鸡视网膜中一种可溶性乳糖结合凝集素的分离与鉴定
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Localization of an endogenous lectin in chicken liver, intestine, and pancreas.一种内源性凝集素在鸡肝脏、肠道和胰腺中的定位。
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引用本文的文献

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Characterization of quail intestinal mucin as a ligand for endogenous quail lectin.鹌鹑肠道黏蛋白作为内源性鹌鹑凝集素配体的特性研究
Biochem J. 1993 Aug 1;293 ( Pt 3)(Pt 3):867-72. doi: 10.1042/bj2930867.
2
Production and characterization of monoclonal antibodies to beta-galactoside-binding lectin of bovine heart muscle. Direct evidence that haemagglutinating activity is associated with a 13kDa protein.牛心肌β-半乳糖苷结合凝集素单克隆抗体的制备与特性鉴定。血凝活性与一种13kDa蛋白相关的直接证据。
Biochem J. 1984 May 15;220(1):253-60. doi: 10.1042/bj2200253.
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Endogenous ligands of rat lung beta-galactoside-binding protein (galaptin) isolated by affinity chromatography on carboxyamidomethylated-galaptin-Sepharose.
通过在羧酰胺甲基化-半乳糖凝集素-琼脂糖上进行亲和层析分离得到的大鼠肺β-半乳糖苷结合蛋白(半乳糖凝集素)的内源性配体。
Biochem J. 1984 Nov 1;223(3):769-74. doi: 10.1042/bj2230769.
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Endogenous lectins from cultured cells: subcellular localization of carbohydrate-binding protein 35 in 3T3 fibroblasts.培养细胞中的内源性凝集素:碳水化合物结合蛋白35在3T3成纤维细胞中的亚细胞定位。
J Cell Biol. 1986 Feb;102(2):477-83. doi: 10.1083/jcb.102.2.477.
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Analysis of sugar-binding sites in mammalian cell nuclei by quantitative flow microfluorometry.通过定量流动微荧光法分析哺乳动物细胞核中的糖结合位点。
Proc Natl Acad Sci U S A. 1986 Aug;83(16):5997-6001. doi: 10.1073/pnas.83.16.5997.
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Endogenous lectins from cultured cells: nuclear localization of carbohydrate-binding protein 35 in proliferating 3T3 fibroblasts.来自培养细胞的内源性凝集素:碳水化合物结合蛋白35在增殖的3T3成纤维细胞中的核定位。
Proc Natl Acad Sci U S A. 1987 Sep;84(18):6452-6. doi: 10.1073/pnas.84.18.6452.
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Evidence that the 14 kDa soluble beta-galactoside-binding lectin in man is encoded by a single gene.有证据表明,人类中14 kDa可溶性β-半乳糖苷结合凝集素由单一基因编码。
Biochem J. 1989 Apr 1;259(1):291-4. doi: 10.1042/bj2590291.
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