Suppr超能文献

HLAMP - 1的部分纯化提供了与心脏间充质形成相关的颗粒基质多组分性质的直接证据。

Partial purification of HLAMP-1 provides direct evidence for the multicomponent nature of the particulate matrix associated with cardiac mesenchyme formation.

作者信息

Sinning A R

机构信息

Department of Anatomy, University of Mississippi Medical Center, Jackson, 39216, USA.

出版信息

J Cell Biochem. 1997 Jul 1;66(1):112-22. doi: 10.1002/(sici)1097-4644(19970701)66:1<112::aid-jcb12>3.0.co;2-l.

Abstract

H-LAMP-1 is a 283 kDa protein that is involved in the transformation of endothelial cells into mesenchyme within the AV canal and proximal outflow tract of the heart. This protein is part of the particulate matrix that has been suggested to be composed of multicomponent complexes that have been termed cardiac adherons. However, to date no direct evidence has been provided that these proteins are complexed into an adheron-like particle. This report provides the first such evidence by showing that purification of hLAMP-1, under gentle conditions, results in the isolation of multiple bands of similar molecular weight within the fractions that contain anti-hLAMP-1 activity.

摘要

H-LAMP-1是一种283 kDa的蛋白质,它参与心脏房室管和近端流出道内内皮细胞向间充质的转化。这种蛋白质是颗粒基质的一部分,有人认为该颗粒基质由多组分复合物组成,这些复合物被称为心脏黏附素。然而,迄今为止,尚未有直接证据表明这些蛋白质会复合形成类似黏附素的颗粒。本报告首次提供了此类证据,表明在温和条件下纯化hLAMP-1会导致在含有抗hLAMP-1活性的组分中分离出多条分子量相似的条带。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验