Electrophoretic Analysis of Reversible Interactions

Nine accessions of Bambara groundnut (Vigna subterranea (L.) Verdc.,syn. Voandzeia subterranea (L.) Thouars ex DC.) obtained from National Centre for Genetic Resources and Biotechnology (NACGRAB), Ibadan, Oyo state, were assessed for their genetic and phylogenetic relatedness through electrophoretic analysis of the seed proteins. 0.2g of the seeds were weighed and macerated with mortar and pestle in 0.2M phosphate buffer containing 0.133M of acid (NaH2PO4) and 0.067 of base (Na2HPO4) at pH 6.5. Protein characterization with standard marker revealed that the seeds of the nine accessions contained proteins (B.S.A, Oval Albumin, Pepsinogen, Trypsinogen and Lysozyme) with molecular weights ranging from 66kda and above, 45 – 65 kDa, 44 – 33 kda, 32-24 kDa and 23-14 kDa, respectively. The student T-test revealed that accessions B, C, E, F, H and I have molecular weights not significantly different from one another (P<0.05) while samples A, D and G showed significantly different values (P>0.05). All the accessions had at least two proteins and two major bands in common. The study revealed intra-specific similarities and genetic diversity in protein contents among the nine accessions of Bambara groundnut (Vigna subterraranea (L.) Verdc.syn

Download Full-text

Future of electrophoretic technology in clinical laboratory testing—From urinary protein electrophoretic analysis to urinary protein pathological analysis—

Electrophoresis Letters ◽

10.2198/electroph.60.23 ◽

2016 ◽

Vol 60 (1) ◽

pp. 23-26

Author(s):

Ryo Kubota ◽

Shiro Iijima ◽

Kiyoko Shiba

Keyword(s):

Laboratory Testing ◽

Clinical Laboratory ◽

Electrophoretic Analysis ◽

Urinary Protein ◽

Pathological Analysis ◽

Clinical Laboratory Testing

Download Full-text

Chromatography-Independent Fractionation and Newly Identified Molecular Features of the Adzuki Bean (Vigna angularis Willd.) β-vignin Protein

International Journal of Molecular Sciences ◽

10.3390/ijms22063018 ◽

2021 ◽

Vol 22 (6) ◽

pp. 3018

Author(s):

Biane Philadelpho ◽

Victória Souza ◽

Fabiani Souza ◽

Johnnie Santos ◽

Fabiana Batista ◽

...

Keyword(s):

Metal Binding ◽

Cardiovascular Health ◽

Binding Capacity ◽

Biological Activities ◽

Electrophoretic Analysis ◽

Adzuki Bean ◽

Molecular Features ◽

Health Promoting ◽

High Degree

Adzuki seed β-vignin, a vicilin-like globulin, has proven to exert various health-promoting biological activities, notably in cardiovascular health. A simple scalable enrichment procedure of this protein for further nutritional and functional studies is crucial. In this study, a simplified chromatography-independent protein fractionation procedure has been optimized and described. The electrophoretic analysis showed a high degree of homogeneity of β-vignin isolate. Furthermore, the molecular features of the purified protein were investigated. The adzuki bean β-vignin was found to have a native size of 146 kDa, and the molecular weight determined was consistent with a trimeric structure. These were identified in two main polypeptide chains (masses of 56–54 kDa) that are glycosylated polypeptides with metal binding capacity, and one minor polypeptide chain with a mass 37 kDa, wherein these features are absent. The in vitro analysis showed a high degree of digestibility of the protein (92%) and potential anti-inflammatory capacity. The results lay the basis not only for further investigation of the health-promoting properties of the adzuki bean β-vignin protein, but also for a possible application as nutraceutical molecule.

Download Full-text