A protein with amino acid sequence homology to bovine insulin is present in the legume Vigna unguiculata (cowpea)
Braz. j. med. biol. res
; 36(9): 1167-1173, Sept. 2003. ilus, tab, graf
Article
in English
| LILACS
| ID: lil-342857
Responsible library:
BR1.1
ABSTRACT
Since the discovery of bovine insulin in plants, much effort has been devoted to the characterization of these proteins and elucidation of their functions. We report here the isolation of a protein with similar molecular mass and same amino acid sequence to bovine insulin from developing fruits of cowpea (Vigna unguiculata) genotype Epace 10. Insulin was measured by ELISA using an anti-human insulin antibody and was detected both in empty pods and seed coats but not in the embryo. The highest concentrations (about 0.5 ng/æg of protein) of the protein were detected in seed coats at 16 and 18 days after pollination, and the values were 1.6 to 4.0 times higher than those found for isolated pods tested on any day. N-terminal amino acid sequencing of insulin was performed on the protein purified by C4-HPLC. The significance of the presence of insulin in these plant tissues is not fully understood but we speculate that it may be involved in the transport of carbohydrate to the fruit
Full text:
Available
Collection:
International databases
Database:
LILACS
Main subject:
Plant Proteins
/
Plants
/
Sequence Homology, Amino Acid
/
Insulin
Limits:
Animals
Language:
English
Journal:
Braz. j. med. biol. res
Journal subject:
Biology
/
Medicine
Year:
2003
Document type:
Article
Affiliation country:
Brazil
Institution/Affiliation country:
Universidade Estadual do Norte Fluminense/BR