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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1994-6-9
|
| pubmed:databankReference | |
| pubmed:abstractText |
The conservation between muscle fatty-acid-binding proteins (M-FABP) of Locusta migratoria flight muscle and human skeletal muscle was investigated. The locust M-FABP cDNA (632 bp) was isolated by 5' and 3' rapid amplification of cDNA ends. The identities of the locust and human M-FABP on the cDNA and protein levels were 54% and 42%, respectively. The predicted amino acid sequence of locust M-FABP indicated a molecular mass of 14935 Da and isoelectric point 6.1. The locust M-FABP was expressed in Escherichia coli, purified by (NH4)2SO4 precipitation, anion-exchange and gel-filtration chromatographies and compared with the recombinant human M-FABP with respect to immunological and binding properties. In spite of the high sequence similarity, the proteins did not show immunological cross-reactivity. The binding parameters of locust M-FABP were analyzed with radiolabeled oleic acid by the Lipidex assay and titration microcalorimetry. Both methods revealed a Kd for oleic acid of 0.5 microM and a binding stoichiometry of 1 mol fatty acid/mol FABP. The delta H, delta G and delta S for oleic acid binding were -146 kJ.mol-1 and -36 J.mol-1 and -369 J.mol-1.K-1 respectively. All the information obtained from binding, fluorescence and displacement studies indicated that locust M-FABP has binding characteristics similar to human M-FABP. Finally the recombinant locust M-FABP was crystallized with and without oleic acid. All crystals were trigonal in the P3(1)21 space group. The unit cell dimensions were a = b = 5.89 nm and c = 14.42 nm.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/FABP7 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acid-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Apr
|
| pubmed:issn |
0014-2956
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
221
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
801-10
|
| pubmed:dateRevised |
2007-7-23
|
| pubmed:meshHeading |
pubmed-meshheading:8174560-Amino Acid Sequence,
pubmed-meshheading:8174560-Animals,
pubmed-meshheading:8174560-Base Sequence,
pubmed-meshheading:8174560-Carrier Proteins,
pubmed-meshheading:8174560-Chromatography, Ion Exchange,
pubmed-meshheading:8174560-Cloning, Molecular,
pubmed-meshheading:8174560-Colorimetry,
pubmed-meshheading:8174560-Crystallography, X-Ray,
pubmed-meshheading:8174560-DNA, Complementary,
pubmed-meshheading:8174560-Escherichia coli,
pubmed-meshheading:8174560-Fatty Acid-Binding Proteins,
pubmed-meshheading:8174560-Fatty Acids,
pubmed-meshheading:8174560-Grasshoppers,
pubmed-meshheading:8174560-Humans,
pubmed-meshheading:8174560-Isoelectric Focusing,
pubmed-meshheading:8174560-Molecular Sequence Data,
pubmed-meshheading:8174560-Molecular Weight,
pubmed-meshheading:8174560-Muscles,
pubmed-meshheading:8174560-Neoplasm Proteins,
pubmed-meshheading:8174560-Sequence Alignment,
pubmed-meshheading:8174560-Sequence Homology, Nucleic Acid,
pubmed-meshheading:8174560-Spectrometry, Fluorescence,
pubmed-meshheading:8174560-Tumor Suppressor Proteins
|
| pubmed:year |
1994
|
| pubmed:articleTitle |
Primary structure and binding characteristics of locust and human muscle fatty-acid-binding proteins.
|
| pubmed:affiliation |
Department of Biochemistry, University of Nijmegen, The Netherlands.
|
| pubmed:publicationType |
Journal Article,
Comparative Study
|