scholarly journals Structure and function of seed storage proteins in faba bean (Vicia faba L.)

3 Biotech ◽  
2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Yujiao Liu ◽  
Xuexia Wu ◽  
Wanwei Hou ◽  
Ping Li ◽  
Weichao Sha ◽  
...  
1988 ◽  
Vol 43 (1-2) ◽  
pp. 149-154 ◽  
Author(s):  
H. Oskar Schmidt

In the course of yellowing (senescence) the leaves of Vicia faba L. lose 95% of their chlorophyll. Gerontoplasts develop from chloroplasts and aggregate with the pycnotic mitochondria and the cell nucleus in the senescent cells (organelle aggregation). The gerontoplasts contain only a few, unstacked thylakoid membranes but a large number of carotinoid-containing plastoglobuli, which after the degration of chlorophyll presumably assume the light protection of the cells. The thylakoid membranes of the gerontoplasts were isolated by means of a flotation method. Their polypeptide composition is characterized by a high proportion of light-harvesting complex. Evidence of relatively high photochemical activity shows that functional thylakoid membranes are present in the premortal senescence state of leaves and this suggests that there is functional compartmentation of the hydrolytic processes in this stage of the leaves’ development


1991 ◽  
Vol 81 (1) ◽  
pp. 50-58 ◽  
Author(s):  
M. Tucci ◽  
R. Capparelli ◽  
A. Costa ◽  
R. Rao

2007 ◽  
Vol 55 (2) ◽  
pp. 131-147
Author(s):  
R. Sammour

In this study, an array of electrophoretic and immunochemical techniques was used to investigate the legumins, vicilins and albumins of seed storage proteins in Pisum sativum , Vicia faba , Lens esculentum , and Cicer arietinum to delimit the boundary of the tribe Vicieae and to clarify the systematic position of the genus Cicer . The band patterns of the legumins of these species were broadly similar in that they had bands at Mr 60 kDa which disappeared in the presence of 2-mercaptoethanol, giving rise to two sets of new bands, at Mr approximately 40 kDa and 20 kDa, representing acidic or α and basic or β subunits. The band patterns of the vicilins were also quite similar in that they showed bands at Mr approximately 71 kDa (convicilin) and 50 kDa (vicilin), which were not altered by the presence of 2-mercaptoethanol. Serologically, the legumins of Vicia faba and Lens esculentum exhibited total identity with Pisum legumin antiserum under nonreducing conditions, whereas the legumin of Cicer arietinum exhibited only partial identity, which was attributed to the failure of the low molecular subunit pair (Mr 33 kDa) to react with Pisum legumin antiserum. On the other hand, the vicilins of Vicia faba , Lens esculentum and Cicer arietinum had only partial identity with the vicilin of Pisum sativum , which was due to the failure of a number of subunits along the electrophoretic patterns of these species to react with Pisum sativum vicilin antiserum. The electrophoretic patterns of Vicia faba , Lens esculentum and Cicer arietinum were markedly different for the albumins. However, immunochemically they gave a positive reaction with Pisum major albumin antiserum (Mr 25 kDa) and showed a band with a molecular weight slightly higher than the major albumin of Pisum sativum . Extending the immunochemical study to members of the Phaseoleae, Glycineae, Cajaneae and Diocleae revealed that the vicilin and legumin of Cicer were more closely related to the Vicieae than to these tribes. Thus the data presented in this work recommended the classification of Cicer under Vicieae rather than as a separate tribe Cicerideae .


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