Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1990-8-16
|
| pubmed:abstractText |
CaPB33 and CaPB37, two annexins purified from bovine brain, interact with a Triton X-100-resistant fraction (cytoskeleton) from bovine brain membranes in a Ca2(+)-dependent way in vitro. The binding is saturable with respect to the CaBP33-CaBP37 concentration, half-maximal binding occurring at approximately 15 micrograms of the CaBP33-CaBP37 mixture/ml. The binding of these two annexins to the crude cytoskeleton preparation as a function of free Ca2+ concentration is biphasic, with half-maximal binding at approximately 50 microM and approximately 400 microM free Ca2+ for the first and the second component, respectively. By an overlay technique, CaBP33 and CaBP37 bind to a set of low Mr polypeptides (10-20 kDa) in the crude cytoskeleton preparation, with formation of an 85-90 kDa complex as investigated in cross-linking experiments. No binding of the CaBP33-CaBP37 mixture to either G- or F-actin has been observed. Identification of the CaBP33-CaBP37-binding proteins in cytoskeletons would help elucidating the function(s) of these annexins in the brain.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
0014-5793
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
2
|
| pubmed:volume |
267
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
171-5
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading | |
| pubmed:year |
1990
|
| pubmed:articleTitle |
Interaction of two brain annexins, CaBP33 and CaBP37, with membrane-skeleton proteins.
|
| pubmed:affiliation |
Department of Experimental Medicine and Biochemical Sciences, University of Perugia, Italy.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|