Linked Life Data

11272850

Source:http://linkedlifedata.com/resource/pubmed/id/11272850

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2001-3-1
pubmed:abstractText
In the early stage of ripening of cherry-tomato fruits (Lycopersicon esculentum var. cherry), the lectin activity increased logarithmically and reached a plateau at day 10 after flowering. During purification of lectin from ripe and unripe fruits, a 42-kDa protein was found abundantly in unripe fruits. The protein cross-reacted with anti-cherry-tomato-lectin serum, retained chitin-binding ability, but showed no lectin activity. Comparative studies between the structure of the lectin and the 42-kDa protein were done. N-Terminal amino acid sequences of the lectin, peptides derived from the S-pyridylethylated lectin, and fragments generated by limited proteolysis of the native lectin showed that the lectin was comprised of three domains, Hyp-rich, Cys-rich, and Gln-rich, and the alignment of them was as this order from the N-terminus. Studies on the 42-kDa protein showed that it contained two of the three domains, Cys-rich and Gln-rich, but the amino acid sequence analysis showed that the protein should be a product of another gene.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0916-8451
pubmed:author
pubmed:issnType
Print
pubmed:volume
65
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
86-93
pubmed:dateRevised
2002-12-13
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Domain construction of cherry-tomato lectin: relation to newly found 42-kDa protein.
pubmed:affiliation
Department of Bioresources Chemistry, Faculty of Horticulture, Chiba University, Matsudo, Japan.
pubmed:publicationType
Journal Article