Open AccessBinding of Ca 2+ influences susceptibility of laminin to proteolytic digestion and interactions between domain‐specific laminin fragments
Author(s) -
PAULSSON Mats,
SALADIN Katrina,
LANDWEHR Ruth
Publication year - 1988
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1988.tb14396.x
Subject(s) - transfer rna , biochemistry , methyltransferase , rna , escherichia coli , enzyme , methionine , methylation , biology , amino acid , microbiology and biotechnology , messenger rna , biosynthesis , chemistry , gene
Ca 2+ was found to influence the patterns of limit digests of laminin obtained with various neutral proteases. In the presence of Ca 2+ , larger fragments were obtained from the central part of laminin than in its absence. This was interpreted as being due to a stabilization of the central short‐arm domains of laminin by bound Ca 2+ . When proteolytic fragments were tested for their ability to aggregate, only large fragments containing intact short arms were active, indicating an important role for these domains in laminin self‐aggregation.