Journal article
Binding of Ca2+ influences susceptibility of laminin to proteolytic digestion and interactions between domain-specific laminin fragments.
- Paulsson M Department of Biophysical Chemistry, University of Basel, Switzerland.
- Saladin K
- Landwehr R
- 1988-11-15
Published in:
- European journal of biochemistry. - 1988
Calcium
Chymotrypsin
Electrophoresis, Polyacrylamide Gel
Fibrinolysin
Laminin
Molecular Weight
Pancreatic Elastase
Peptide Fragments
Protein Binding
English
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.
- Language
-
- English
- Open access status
- closed
- Identifiers
-
- DOI 10.1111/j.1432-1033.1988.tb14397.x
- PMID 2973983
- Persistent URL
- https://sonar.ch/global/documents/47073
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