Abstract:
:Two lectins were purified by affinity chromatography from mature peanut (Arachis hypogaea L.) nodules, and compared with the previously characterised seed lectin of this plant. One of the nodule lectins was similar to the seed lectin in its molecular weight and amino-acid composition and ability to bind derivatives of galactose. However, unlike the seed lectin, this nodule lectin appeared to be a glycoprotein and the two lectins were only partially identical in their reaction with antibodies prepared against the seed lectin. The other nodule lectin also appeared to be a glycoprotein but bound mannose/glucose-like sugar derivatives, and differed from the seed lectin in molecular weight, antigenic properties and amino-acid composition.
journal_name
Plantajournal_title
Plantaauthors
Law IJ,Haylett T,Strijdom BWdoi
10.1007/BF00392475subject
Has Abstractpub_date
1988-11-01 00:00:00pages
19-27issue
1eissn
0032-0935issn
1432-2048journal_volume
176pub_type
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