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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1996-11-27
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pubmed:abstractText |
Isolation, purification, amino acid sequence determination and X-ray crystal structure of buffalo alpha-lactalbumin were performed in order to gain further knowledge of the molecular basis of alpha-lactalbumin in the lactose synthase complex. The deduced amino acid sequence differs at one position from the bovine alpha-lactalbumin sequence (at position 17). The refined crystal structure at 2.3 A is very similar to those previously reported for human and baboon alpha-lactalbumins. However, a portion of the molecule (residues 105-109) exhibits different conformation. It forms a 'flexible loop', and appears to be a functionally important region in forming the lactose synthase complex.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
394
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
91-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8925936-Amino Acid Sequence,
pubmed-meshheading:8925936-Animals,
pubmed-meshheading:8925936-Buffaloes,
pubmed-meshheading:8925936-Chromatography,
pubmed-meshheading:8925936-Crystallography, X-Ray,
pubmed-meshheading:8925936-Lactalbumin,
pubmed-meshheading:8925936-Mass Spectrometry,
pubmed-meshheading:8925936-Models, Molecular,
pubmed-meshheading:8925936-Molecular Sequence Data,
pubmed-meshheading:8925936-Protein Conformation,
pubmed-meshheading:8925936-Sequence Analysis,
pubmed-meshheading:8925936-Sequence Homology, Amino Acid
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pubmed:year |
1996
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pubmed:articleTitle |
Amino acid sequence and crystal structure of buffalo alpha-lactalbumin.
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pubmed:affiliation |
School of Biology and Biochemistry, University of Bath, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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