Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
|
pubmed:dateCreated |
1984-7-2
|
pubmed:abstractText |
Human erythrocyte ankyrin was cleaved by restricted proteolysis at 0 degrees C into two distinct chemical domains. The site on ankyrin that binds spectrin was found to be within a 55,000-dalton domain by spectrin affinity chromatography and co-sedimentation with spectrin in a sucrose gradient. A 32,000-dalton fragment of this domain was prepared (tryptic digest, 0 degrees C, 24 h), separated by gel filtration, and shown to inhibit spectrin binding to the membrane. By comparison with previous two-dimensional peptide maps, the spectrin-binding site was located within this 32,000-dalton fragment near the end of the molecule. The band 3-binding site was identified within an 82,000-dalton domain by binding to a band 3 affinity column. Gel electrophoresis in the absence of detergents confirmed these results and demonstrated that a peptide from the cytoplasmic portion of band 3 retained the capacity to bind the 82,000-dalton domain. The binding properties of the structural domains of ankyrin were correlated with a determination of the affinity constant of the intact molecule. Ankyrin bound with a high affinity to the cytoplasmic portion of band 3 (KD = 8 X 10(-8) M) and to spectrin tetramer (KD = 1 X 10(-7) M) but less so to spectrin dimer (KD = 1 X 10(-6) M). These findings are summarized in a preliminary structural and functional model of ankyrin's role in linking spectrin to the membrane.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anion Exchange Protein 1...,
http://linkedlifedata.com/resource/pubmed/chemical/Ankyrins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Spectrin
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0021-9258
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
25
|
pubmed:volume |
259
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
6170-5
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:6233274-Anion Exchange Protein 1, Erythrocyte,
pubmed-meshheading:6233274-Ankyrins,
pubmed-meshheading:6233274-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:6233274-Erythrocyte Membrane,
pubmed-meshheading:6233274-Humans,
pubmed-meshheading:6233274-Kinetics,
pubmed-meshheading:6233274-Membrane Proteins,
pubmed-meshheading:6233274-Peptide Fragments,
pubmed-meshheading:6233274-Protein Binding,
pubmed-meshheading:6233274-Spectrin
|
pubmed:year |
1984
|
pubmed:articleTitle |
The structural basis of ankyrin function. II. Identification of two functional domains.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|