Napin

Napin is one of the two most abundant seed storage proteins in mustard and rapeseed (Brassica napus L., B. juncea L. Czern., B. nigra L. W.D.J.Koch, B. rapa L. and Sinapis alba L.).[1] They are water soluble low-molecular weight basic proteins classified as 2S or 1.7S proteins, representing 20–40% of total seed protein, and having a molecular weight in the range of 12–17 kDa.[2][3] Their isoelectric point varies based on the method of extraction and the specific characteristics of the isoforms that exist. They are composed of two polypeptide chains, a 4.5 kDa small subunit and a large 10 kDa subunit, stabilized primarily by disulphide bonds. Their secondary structure shows a high α-helical content.[4]

References
  1. Rahman, M. (2018). "Brassicaceae mustards: Traditional and agronomic uses in Australia and New Zealand". Molecules. 23 (1): 231. doi:10.3390/molecules23010231. PMC 6017612. PMID 29361740.
  2. Rahman, M. (2000). "In Silico, Molecular Docking and In Vitro Antimicrobial Activity of the Major Rapeseed Seed Storage Proteins". Frontiers in Pharmacology. 11. doi:10.3389/fphar.2020.01340. This article incorporates text available under the CC BY 4.0 license.
  3. Rahman, M. (2000). "Identification, characterization and epitope mapping of proteins encoded by putative allergenic napin genes from Brassica rapa". Clinical and Experimental Allergy. 50 (7): 848–868. doi:10.1111/cea.13612. PMID 32306538. S2CID 216029445.
  4. Rahman, M. (2000). "In Silico, Molecular Docking and In Vitro Antimicrobial Activity of the Major Rapeseed Seed Storage Proteins". Frontiers in Pharmacology. 11. doi:10.3389/fphar.2020.01340.


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