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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1990-3-20
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pubmed:abstractText |
Pigeonpea (Cajanus cajan) vicilin (Mr 190 kD) holoprotein contains 2 subunits and the N-terminal amino acid sequence is Gly-Ala-Arg-Val-Asp-Gln-Glu for purified vicilin subunit 1 (Mr 72 kD) and Thr-Thr-Cys-Met-Glu-Ser-Gly for purified vicilin subunit 2 (Mr 57 kD). Circular dichroism spectra of vicilin indicate the occurrence of a predominant beta- pleated sheet structure. The fluorescence studies of vicilin reveal its unusual stability to 8 M urea and 6 M guanidine HCl.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
166
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1446-52
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:2306256-Amino Acid Sequence,
pubmed-meshheading:2306256-Circular Dichroism,
pubmed-meshheading:2306256-Fabaceae,
pubmed-meshheading:2306256-Macromolecular Substances,
pubmed-meshheading:2306256-Molecular Sequence Data,
pubmed-meshheading:2306256-Peptide Mapping,
pubmed-meshheading:2306256-Plant Proteins,
pubmed-meshheading:2306256-Plants, Medicinal,
pubmed-meshheading:2306256-Protein Denaturation,
pubmed-meshheading:2306256-Seed Storage Proteins,
pubmed-meshheading:2306256-Spectrometry, Fluorescence,
pubmed-meshheading:2306256-Vegetable Proteins
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pubmed:year |
1990
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pubmed:articleTitle |
Unusual denaturation properties of vicilin from Cajanus cajan.
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pubmed:affiliation |
Division of Biochemical Sciences, National Chemical Laboratory, (Maharashtra), India.
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pubmed:publicationType |
Journal Article
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