Expression of A/B zeins in single and double maize endosperm mutants

1992 ◽  
Vol 85 (4) ◽  
pp. 407-414 ◽  
Author(s):  
J. W. Paulis ◽  
J. A. Bietz ◽  
T. P. Bogyo ◽  
T. C. Nelsen ◽  
L. L. Darrah ◽  
...  
Crop Science ◽  
1974 ◽  
Vol 14 (5) ◽  
pp. 676-678
Author(s):  
D. L. Garwood ◽  
J. S. Shenk ◽  
R. F. Barnes

2004 ◽  
Vol 31 (4) ◽  
pp. 339 ◽  
Author(s):  
Ricardo A. Azevedo ◽  
Catherine Damerval ◽  
Peter J. Lea ◽  
Jacques Landry ◽  
Cláudia M. Bellato ◽  
...  

The capacity of three maize endosperm opaque mutants (o10, o11 and o13) to accumulate soluble lysine in the seed in relation to their wildtype counterpart, W22+, was investigated. The W22o13 and W22o11 mutants exhibited 278% and 186% increases in soluble lysine, respectively, while for W22o10, a 36% decrease was observed, compared with the wildtype. A quantitative and qualitative study of the N constituents of the endosperm has been conducted and data obtained for the total protein, non-protein N, soluble amino acids, albumins / globulins, zeins and glutelins present in the seed of the mutants. Following 2D–PAGE, a total of 38 different forms of zein polypeptides were detected and considerable differences were noted between the three mutant lines. The metabolism of lysine was also studied by analysis of the enzymes aspartate kinase, homoserine dehydrogenase, lysine 2-oxoglutarate reductase and saccharopine dehydrogenase, which exhibited major changes in activity, depending on the genotype, suggesting that the mutant genes may have distinct regulatory activities.


Crop Science ◽  
1978 ◽  
Vol 18 (5) ◽  
pp. 709-712 ◽  
Author(s):  
D. E. Rowe ◽  
D. L. Garwood

2003 ◽  
Vol 60 (1) ◽  
pp. 91-96 ◽  
Author(s):  
Alejandro Alberto Toro ◽  
Leonardo Oliveira Medici ◽  
Ladaslav Sodek ◽  
Peter John Lea ◽  
Ricardo Antunes Azevedo

For human nutrition the main source of vegetable proteins are cereal and legume seeds. The content of total soluble amino acids in mature endosperm of wild-type, opaque and floury maize (Zea mays L.) mutants were determined by HPLC. The total absolute concentration of soluble amino acids among the mutants varied depending on the mutant. The o11 and o13 mutants exhibited the highest average content, whereas o10, fl3 and fl1 exhibited the lowest average content. In general, the mutants exhibited similar concentrations of total soluble amino acids when compared to the wild-type lines, with the clear exception of mutants o11 and fl1, with the o11 mutant exhibiting a higher concentration of total soluble amino acids when compared to its wild-type counterpart W22 and the fl1 mutant a lower concentration when compared to its wild-type counterpart Oh43. For methionine, the mutants o2 and o11 and wild-type Oh43 exhibited the highest concentrations of this amino acid. Significant differences were not observed between mutants for other amino acids such as lysine and threonine. The high lysine concentrations obtained originally for these mutants may be due to the amino acids incorporated into storage proteins, but not those present in the soluble form.


1981 ◽  
Vol 33 (7) ◽  
pp. 222-230 ◽  
Author(s):  
J. Y. Yeh ◽  
D. L. Garwood ◽  
J. C. Shannon

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