Mungbean [Vigna radiata (L.) Wilczek] globulins: Purification and characterization

Citation
Emt. Mendoza et al., Mungbean [Vigna radiata (L.) Wilczek] globulins: Purification and characterization, J AGR FOOD, 49(3), 2001, pp. 1552-1558
Citations number
34
Categorie Soggetti
Agricultural Chemistry","Chemistry & Analysis
Journal title
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
ISSN journal
00218561 → ACNP
Volume
49
Issue
3
Year of publication
2001
Pages
1552 - 1558
Database
ISI
SICI code
0021-8561(200103)49:3<1552:M[R(WG>2.0.ZU;2-8
Abstract
Vicilin type (8S) and basic 7S globulins and legumin type (11S) globulins w ere isolated from mungbean [Vigna radiata (L.) Wilczek]. The native molecul ar weights of the different globulin types were 360000 for legumin, 200000 for vicilin, and 135000 for basic 7S. Some of the 8S globulin apparently co mplexed and coeluted with the 11S on gel filtration. On SDS-PAGE, 11S was c omposed of two bands of 40000 and 24000, 8S was composed of 60000, 48000, 3 2000, and 26000 bands, and basic 7S was composed of 28000 and 16000 bands. The percent composition of total globulins was estimated to be as follow: 8 S, 89%; basic 7S, 3.4%; and 11S, 7.6%. The basic 7S and 11S but not the 8S globulins were found to have disulfide bonds. The presence of carbohydrates by conjugated peroxidase reaction was observed in all bands of 8S, the aci dic polypeptide of basic 7S, and its complex but not in 11S, The 28000 basi c 7S band and its 42000 complex and the first three major bands of 8S cross -reacted with antibodies to all types of soybean conglycinin subunits (alph a, alpha ', and beta), whereas the fourth band cross-reacted only with the anti-beta subunit. None of the mungbean globulins crossreacted with anti-so ybean glycinin. Basic 7S was found to be easily extracted with 0.15 M NaCl, 11S was extracted with 0.35 M NaCl,and 8S was extracted over a wide range of NaCl concentrations. The N-terminal sequences of the different subunits/ fragments of the globulins were determined and found to have strong;homolog y with storage proteins of other legumes and crops.