Editing Lectin (section)

===Plants===
The function of lectins in plants ([[legume lectin]]) is still uncertain. Once thought to be necessary for [[rhizobia]] binding, this proposed function was ruled out through lectin-knockout [[transgene]] studies.<ref>{{Cite journal |title=Coordinating Nodule Morphogenesis with Rhizobial Infection in Legumes |journal=Annual Review of Plant Biology |volume=59 |pages=519–546 |doi=10.1146/annurev.arplant.59.032607.092839 |pmid=18444906 |year=2008 |last1=Oldroyd |first1=Giles E.D. |last2=Downie |first2=J. Allan}}</ref>

The large concentration of lectins in plant seeds decreases with growth, and suggests a role in plant [[germination]] and perhaps in the seed's survival itself. The binding of glycoproteins on the surface of parasitic cells also is believed to be a function. Several plant lectins have been found to recognize noncarbohydrate [[ligands]] that are primarily [[hydrophobic]] in nature, including [[adenine]], [[auxins]], [[cytokinin]], and [[indole acetic acid]], as well as water-soluble [[porphyrins]]. These interactions may be physiologically relevant, since some of these molecules function as [[phytohormone]]s.<ref name="pmid16525538">{{cite journal |vauthors=Komath SS, Kavitha M, Swamy MJ |title=Beyond carbohydrate binding: new directions in plant lectin research |journal=Org. Biomol. Chem. |volume=4 |issue=6 |pages=973–988 |date=March 2006 |pmid=16525538 |doi=10.1039/b515446d}}</ref>

Lectin receptor kinases (LecRKs) are believed to recognize damage associated molecular patterns (DAMPs), which are created or released from herbivore attack.{{cn|date=May 2021}} In ''[[Arabidopsis]]'', legume-type LecRKs Clade 1 has 11 LecRK proteins. LecRK-1.8 has been reported to recognize extracellular [[Nicotinamide adenine dinucleotide|NAD]] molecules and LecRK-1.9 has been reported to recognize extracellular [[Adenosine triphosphate|ATP]] molecules.{{cn|date=May 2021}}

Extraction of proteins and lectins can be extracted via similar processes, also with their analysis, and discovery. For example [[cottonseed]]  contains compounds of interest within the studies of extraction and purification of proteins<ref> L.Y. Yatsu, T.J. Jacks, "Association of lysosomal activity with aleurone grains in plant seeds", ''Archives of Biochemistry and Biophysics'', Vol. 124, 1968, pp. 466–471, {{ISSN|0003-9861}}, {{doi|10.1016/0003-9861(68)90354-8}}.</ref>