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:	05 Dec 2022 14:33
Publisher DOI:	10.1006/abio.1994.1465
PubMed ID:	7856840
URI:	https://boris.unibe.ch/id/eprint/50164