Abstract
Ca2+ was found to influence the patterns of limit digests of laminin obtained with various neutral proteases. In the presence of Ca2+, 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 Ca2+. 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.
References
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Dates
Type | When |
---|---|
Created | 20 years, 5 months ago (March 3, 2005, 9:38 p.m.) |
Deposited | 1 year, 10 months ago (Oct. 31, 2023, 11:33 a.m.) |
Indexed | 1 year, 4 months ago (April 15, 2024, 11:09 a.m.) |
Issued | 36 years, 10 months ago (Nov. 1, 1988) |
Published | 36 years, 10 months ago (Nov. 1, 1988) |
Published Online | 20 years, 6 months ago (March 3, 2005) |
Published Print | 36 years, 10 months ago (Nov. 1, 1988) |
@article{PAULSSON_1988, title={Binding of Ca2+ influences susceptibility of laminin to proteolytic digestion and interactions between domain‐specific laminin fragments}, volume={177}, ISSN={1432-1033}, url={http://dx.doi.org/10.1111/j.1432-1033.1988.tb14396.x}, DOI={10.1111/j.1432-1033.1988.tb14396.x}, number={3}, journal={European Journal of Biochemistry}, publisher={Wiley}, author={PAULSSON, Mats and SALADIN, Katrina and LANDWEHR, Ruth}, year={1988}, month=nov, pages={477–481} }