Physiological changes in the early stages of germination of pea seeds induced by aging and by infection by a storage fungus, Aspergillus ruber

1976 ◽  
Vol 54 (1-2) ◽  
pp. 39-44 ◽  
Author(s):  
G. E. Harman ◽  
A. A. Khan ◽  
K. L. Tao
Keyword(s):  
Alkaline Phosphatase ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Relative Humidity ◽  
Physiological Changes ◽  
Embryonic Axes ◽  
Storage Fungi ◽  
Storage Fungus ◽  
Pea Seeds ◽  
Reduced Activity

Pea seeds age rapidly and may be infected by storage fungi, e.g. Aspergillus ruber, when stored under conditions of high relative humidity and temperature (92% relative humidity and 30 °C in these experiments). In the absence of microorganisms, pea seeds retain their viability for 6 to 8 weeks, although the speed of germination is reduced. In embryonic axes, aging is associated with a slower increase in O2 uptake, a delay in protein synthesis, smaller ATP and amino acid pools, and reduced activity of alkaline phosphatase (EC 3.1.3.1) and 3-phosphoglyceraldelyde dehydrogenase (EC 1.2.1.12). Axes recover from these changes during germination. Infection by A. ruber reduces germination. In axes from infected peas the onset of protein synthesis is delayed even more and the ATP and amino acid pools are smaller than in aged axes. Axes from infected seeds recover slowly, if at all.

The volatile exudates from germinating pea seeds of different viability and vigor

1985 ◽  
Vol 63 (6) ◽  
pp. 1035-1039 ◽  
Author(s):  
R. J. Gorecki ◽  
G. E. Harman ◽  
L. R. Mattick
Keyword(s):  
Gas Chromatography ◽  
Relative Humidity ◽  
Trichoderma Harzianum ◽  
Storage Time ◽  
Enterobacter Cloacae ◽  
Storage Condition ◽  
Seed Vigor ◽  
Embryonic Axes ◽  
Pea Seeds ◽  
Germinating Seeds

Pea seeds var. Kriter were stored aseptically at 92% relative humidity and 30 °C. After 0, 4, 6, 8, or 10 weeks of storage, viability, vigor, and volatile exudates were determined on sublots of seeds. As storage time increased, vigor, as measured by dehydrogenase activity, growth of embryonic axes, and conductivity decreased. Later, viability also decreased. Imbibing and germinating pea seeds produced ethanol, acetaldehyde, and lesser amounts of methanol. No qualitative differences in volatile exudates were observed from germinating seeds regardless of age or storage condition. Nonaged seeds with highest vigor produced the smallest amounts of volatiles, but with increased aging the quantities of ethanol and acetaldehyde gradually increased. Dry seed produced small quantities of both volatiles. The amount of these compounds produced reached a maximum between 12 and 48 h of germination. Infestation of seed samples with Enterobacter cloacae or Trichoderma harzianum reduced the quantities of these compounds measured. These results indicate that determinations of acetaldehyde and ethanol in the space over germinating seeds by means of gas chromatography may be a useful seed vigor test.

scholarly journals Identification of Mimotope Peptides Which Bind to the Mycotoxin Deoxynivalenol-Specific Monoclonal Antibody

1999 ◽  
Vol 65 (8) ◽  
pp. 3279-3286 ◽  
Author(s):  
Qiaoping Yuan ◽  
James J. Pestka ◽  
Brandon M. Hespenheide ◽  
Leslie A. Kuhn ◽  
John E. Linz ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Alkaline Phosphatase ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Synthetic Peptide ◽  
Amino Acid Sequences ◽  
In Vitro Translation ◽  
Enzyme Linked Immunosorbent Assay ◽  
Translation System

ABSTRACT Monoclonal antibody 6F5 (mAb 6F5), which recognizes the mycotoxin deoxynivalenol (DON) (vomitoxin), was used to select for peptides that mimic the mycotoxin by employing a library of filamentous phages that have random 7-mer peptides on their surfaces. Two phage clones selected from the random peptide phage-displayed library coded for the amino acid sequences SWGPFPF and SWGPLPF. These clones were designated DONPEP.2 and DONPEP.12, respectively. The results of a competitive enzyme-linked immunosorbent assay (ELISA) suggested that the two phage displayed peptides bound to mAb 6F5 specifically at the DON binding site. The amino acid sequence of DONPEP.2 plus a structurally flexible linker at the C terminus (SWGPFPFGGGSC) was synthesized and tested to determine its ability to bind to mAb 6F5. This synthetic peptide (designated peptide C430) and DON competed with each other for mAb 6F5 binding. When translationally fused with bacterial alkaline phosphatase, DONPEP.2 bound specifically to mAb 6F5, while the fusion protein retained alkaline phosphatase activity. The potential of using DONPEP.2 as an immunochemical reagent in a DON immunoassay was evaluated with a DON-spiked wheat extract. When peptide C430 was conjugated to bovine serum albumin, it elicited antibody specific to peptide C430 but not to DON in both mice and rabbits. In an in vitro translation system containing rabbit reticulocyte lysate, synthetic peptide C430 did not inhibit protein synthesis but did show antagonism toward DON-induced protein synthesis inhibition. These data suggest that the peptides selected in this study bind to mAb 6F5 and that peptide C430 binds to ribosomes at the same sites as DON.

scholarly journals Proteins in pea seeds after 7 months of storage at 50 and 90% relative humidity

2014 ◽  
Vol 54 (4) ◽  
pp. 367-378
Author(s):  
Ryszard J. Górecki ◽  
Andrzej Klasa ◽  
Artur Bałajewicz
Keyword(s):  
Relative Humidity ◽  
Gel Electrophoresis ◽  
Room Temperature ◽  
Polyacrylamide Gel Electrophoresis ◽  
Electrophoretic Pattern ◽  
Embryonic Axes ◽  
Albumin Content ◽  
Pea Seeds ◽  
Viable Seeds ◽  
Pea Seed

Two pea seed lots var. Flavanda were stored at 50 and 90% relative humidity (r.h.) at room temperature. After 7 months the germinability of seeds stored at 90% r.h. was reduced to 19%;. Similarly, the vigor of these seeds was lower as compared with seeds stored at 50% r.h. Deterioration of seeds resulted in the reduction of the albumin content from about 14 to 8 mg per seed. The content of vicillin in non-viable seeds was twice as high than in fully vigorous ones. No changes in the level of legumin appeared. During germination of seeds with lowered viability and vigor, the protein content of their embryonic axes did not increase. Polyacrylamide gel electrophoresis of protein extracted from the cotyledons of aged seeds showed visible changes only in the electrophoretic pattern of the albumin fraction.

scholarly journals PROTEIN SYNTHESIS AND AMINO ACID TURNOVER IN TISSUE CULTURE

1952 ◽  
Vol 196 (1) ◽  
pp. 51-68 ◽  
Author(s):  
H.W. Gerarde ◽  
Marion. Jones ◽  
Theodore. Winnick
Keyword(s):  
Tissue Culture ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Amino Acid Turnover
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