Affinity retardation chromatography: characterization of the method and its application. The description of low affinity laminin self-interactions.

Schittny, Johannes (1994). Affinity retardation chromatography: characterization of the method and its application. The description of low affinity laminin self-interactions. Analytical biochemistry, 222(1), pp. 140-148. Elsevier 10.1006/abio.1994.1465

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Affinity retardation chromatography (ARC), a method for the examination of low-affinity interactions, is mathematically described in order to characterize the method itself and to estimate binding coefficients of self-assembly domains of basement membrane protein laminin. Affinity retardation was determined by comparing the elutions on a "binding" and on a "nonreacting" column. It depends on the binding coefficient, the concentrations of both ligands, and the nonbinding elution position. Half maximal binding of the NH2-terminal domain of laminin B1-short arm to the A- and/or B2-short arms was estimated to occur at 10-17 microM for noncooperative and at < or = 3 microM for cooperative binding. A model of the laminin polymerization, postulating two levels of cooperative binding behavior, is described.

Item Type:

Journal Article (Original Article)

Division/Institute:

04 Faculty of Medicine > Pre-clinic Human Medicine > Institute of Anatomy > Functional Anatomy

UniBE Contributor:

Schittny, Johannes

Subjects:

500 Science > 570 Life sciences; biology

ISSN:

0003-2697

Publisher:

Elsevier

Language:

English

Submitter:

Johannes Schittny

Date Deposited:

18 Aug 2014 16:38

Last Modified:

18 Aug 2014 16:38

Publisher DOI:

10.1006/abio.1994.1465

PubMed ID:

7856840

URI:

https://boris.unibe.ch/id/eprint/50164

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