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Partial purification of HLAMP‐1 provides direct evidence for the multicomponent nature of the particulate matrix associated with cardiac mesenchyme formation
Author(s) -
Sinning Allan R.
Publication year - 1997
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/(sici)1097-4644(19970701)66:1<112::aid-jcb12>3.0.co;2-l
Subject(s) - mesenchyme , particulates , matrix (chemical analysis) , chemistry , microbiology and biotechnology , biochemistry , biology , chromatography , organic chemistry , embryo
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. J. Cell. Biochem. 66:112–122, 1997. © 1997 Wiley‐Liss, Inc.