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.

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.

Milk Films Exposed to High Humidity: Studies with Electron Microscopy and Electrophoresis1,2

1980 ◽  
Vol 43 (1) ◽  
pp. 29-35 ◽  
Author(s):  
R. C. MABESA ◽  
R. T. MARSHALL ◽  
M. E. ANDERSON
Keyword(s):  
Electron Microscopy ◽  
Relative Humidity ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Raw Milk ◽  
Steel Plates ◽  
High Humidity ◽  
Residual Film ◽  
Contact Surfaces ◽  
Scanning Electron

Stainless steel plates, which are similar to milk contact surfaces, were dipped in fresh raw milk. The residual film was dried (37 C and 10% to 20% relative humidity) for 30 min. Treated plates were then exposed to 100% relative humidity for 30 min at 37 C. Scanning electron microscopy revealed splotches of fat on surfaces of dried films and the humidified films had a more aggregated and porous appearance than films that were dried only. The incidence of granulated lactose was greater among humidified samples than among nonhumidified samples. Discontinuous polyacrylamide gel electrophoresis revealed that α- and β-caseins resisted rinsing from plates on which dried films were exposed to 100% relative humidity but not from plates on which films had been dried only.

scholarly journals Viability and vigour of ageing pea seeds with various densities

2014 ◽  
Vol 51 (3-4) ◽  
pp. 481-488
Author(s):  
Ryszard J. Górecki
Keyword(s):  
Specific Gravity ◽  
Growth Analysis ◽  
Germination Rate ◽  
Air Humidity ◽  
Embryonic Axes ◽  
Dry Air ◽  
Relative Air Humidity ◽  
Pea Seeds ◽  
Sprout Growth ◽  
Pea Seed

Pea seed lots (of big and small densities and a control) were stored for six months in hydrostats in relative air humidity 90 and 50 per cent, at 21°C. Viability was determined on the basis of germination rate (energy) and capacity; vigour on the basis of sprout growth analysis, conductometric measurements and over-all dehydrogenase activity in the embryonic axes (tigella). Seeds stored in a high relative air humidity were losimg their viability and vigour more quickly than did those stored in a dry air. Seeds of big density were preserving better and ageing slower than seeds of small specific gravity.

Glycoproteins, enzymatic activities, and b proteins in intercellular fluid extracts from hypersensitive Nicotiana species infected with tobacco mosaic virus

1985 ◽  
Vol 63 (5) ◽  
pp. 928-931 ◽  
Author(s):  
Jean-Guy Parent ◽  
Richard Hogue ◽  
Alain Asselin
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Electrophoretic Pattern ◽  
Protein Band ◽  
Polyacrylamide Gel ◽  
Intercellular Fluid ◽  
Nicotiana Tabacum L ◽  
The One

Intercellular fluid b proteins from hypersensitive Nicotiana tabacum L. cv. Xanthi-nc and N. sylvestris Speg. and Comes infected with tobacco mosaic virus were compared by two-dimensional (2-D) polyacrylamide gel electrophoresis. Except for missing bands b2, b6a, b6b, and b7b, the overall 2-D electrophoretic pattern of N. sylvestris intercellular fluid proteins was similar to the one observed with 'Xanthi-nc' tobacco. Intercellular proteins were also studied by chromatography on con-canavalin A. Glycoproteins corresponding to b6a and b7a proteins of N. tabacum and the [Formula: see text] analog of N. sylvestris were identified. These proteins are probably peroxidase isozymes, as peroxidase activities with the same electrophoretic mobility were detected after polyacrylamide gel electrophoresis. No esterase activity was associated with any b protein band in gels. Esterase activities decreased upon virus infection, but accumulation of b proteins and peroxidase activities increased.

BARLEY CULTIVAR IDENTIFICATION BY ELECTROPHORETIC ANALYSIS OF HORDEIN PROTEINS: I. EXTRACTION AND SEPARATION OF HORDEIN PROTEINS AND ENVIRONMENTAL EFFECTS ON THE HORDEIN ELECTROPHOREGRAM

1980 ◽  
Vol 60 (4) ◽  
pp. 1343-1350 ◽  
Author(s):  
B. A. MARCHYLO ◽  
D. E. LaBERGE
Keyword(s):  
Gel Electrophoresis ◽  
Room Temperature ◽  
Cultivar Identification ◽  
Polyacrylamide Gel Electrophoresis ◽  
Electrophoretic Analysis ◽  
Western Canada ◽  
Barley Cultivar ◽  
Barley Cultivars ◽  
Extraction And Separation ◽  
Acid Gel

Reproducible hordein electrophoregrams were obtained when hordeins, extracted from Canadian-grown barley cultivars, were subjected to polyacrylamide gel electrophoresis at acid pH (acid-gel PAGE). The hordeins were extracted at room temperature into a solution of 55% (vol/vol) isopropanol containing 2% (vol/vol) monothioglycerol. Extraction of hordein at high temperature (60 °C) produced significant reduction in the number of protein bands available for cultivar identification. Alkylation of the reduced hordeins, prior to acid-gel PAGE, did not improve the resolution or appearance of the hordein electrophoregrams. The effect of environment on the hordein electrophoregram was studied. Four barley cultivars were grown at eight locations in Western Canada during 2 successive years. Hordein electrophoregrams were qualitatively independent of growth location, year of growth and protein content. These results suggest that acid-gel PAGE should prove useful as a technique for barley cultivar identification.

Purification and Characterization of an Unusual Aminopeptidase From Pea Seeds

1980 ◽  
Vol 7 (2) ◽  
pp. 131 ◽  
Author(s):  
JB Caldwell ◽  
LG Sparrow
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Sulfhydryl Group ◽  
Purification And Characterization ◽  
Apparent Homogeneity ◽  
Pea Seeds ◽  
Hydrolysis Of

An aminopeptidase with specificity for N-terminal glutamic and aspartic acid residues has been purified to apparent homogeneity from pea seeds (Pisum sativum cv. Greenfeast). It also catalyses the hydrolysis of the glutaryl-phenylalanine bond of the synthetic chymotrypsin substrate glutaryl- L-phenylalanine p-nitroanilide. The native enzyme, which has a molecular weight of approximately 500 000, gives a single band on polyacrylamide gel electrophoresis but two major bands when subjected to electrophoresis in the presence of sodium dodecyl sulfate after reduction. Its behaviour with various inhibitors suggests that a sulfhydryl group is important for its activity.

Detección inmunoquímica de la adulteración de chorizo de cerdo con proteínas de soja

1998 ◽  
Vol 4 (4) ◽  
pp. 257-262 ◽  
Author(s):  
A.F. González-Córdova ◽  
A.M. Calderón de la Barca ◽  
M. Cota ◽  
B. Vallejo-Córdoba
Keyword(s):  
Gel Electrophoresis ◽  
Protein Extraction ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Electrophoretic Pattern ◽  
Soy Flour ◽  
Nacl Solution ◽  
Standard Curve ◽  
Sds Page ◽  
Polyclonal Antisera

Rabbit polyclonal antisera were produced against soy flour proteins extracted with 0.5 M NaCl solution and purified by affinity chromatography to detect adulteration in pork chorizo (sausage) with an enzyme-linked immunoabsorbent assay (ELISA). To detect adulteration the following saline extracts were prepared: 100% pork and 100% soy chorizo and mixtures of these two pro ducts (90:10, 80:20, 70:30, 60:40, 50:50, 40:60, 30:70, 20:80, 10:90), and extracts of two commercial chorizos labeled as pork. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) showed that the salt solution was the most suitable for protein extraction compared to water and a 1% SDS solution. The commercial chorizos did not have the characteristic electrophoretic pattern for pork chorizos. The antibodies were specific for soy and its products, as there was no response to other vegetable and animal proteins by gel immunodiffusion assay or ELISA. The standard curve obtained with the ELISA results of the chorizo mixtures gave a correlation coefficient of r2 = 0.988. The two commercial chorizo values resulted in a 32 and 40% soy substitution. Total time for ELISA was optimized to 4 h, and 2 h if the plates were previously activated with the antigen. Variation coefficients of ELISA readings for replicates of the same extract in one plate and variation of different assays on different days were 2.3 and 8% respectively.

Isoenzyme and protein patterns of pentose-fermenting yeasts

1987 ◽  
Vol 33 (11) ◽  
pp. 1017-1023 ◽  
Author(s):  
Robert S. Jeng ◽  
Shiyuan Yu ◽  
Morris Wayman
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Electrophoretic Pattern ◽  
Pichia Stipitis ◽  
Culture Collection ◽  
Polyacrylamide Gel ◽  
The Other ◽  
Two Dimensional ◽  
Protein Patterns

Soluble proteins were extracted from the vegetative cells of four pentose-fermenting yeasts, Candida shehatae, Pichia stipitis, R-1, and R-2, the R strains being of uncertain taxonomy, while the other two are culture collection yeasts. Isoenzyme patterns, protein patterns, and two-dimensional polypeptide mapping of these four strains were compared by polyacrylamide gel electrophoresis. The two R strains showed great similarity in two-dimensional polypeptide mapping, the pattern of sodium dodecyl sulfate – polyacrylamide gel electrophoresis, isoelectrofocusing, and isoenzymes, and may be one species. Each of the other two yeasts had its own characteristic electrophoretic pattern. The R strains showed the presence of three alcohol dehydrogenase isoenzymes compared with one for the culture collection yeasts, as well as much higher activity of malate dehydrogenase, isocitrate dehydrogenase, glucose-6-phosphate dehydrogenase, and 6-phosphogluconate dehydrogenase, which further the formation of pyruvate and ethanol.

A case of proteinuria with analbuminuria.

1985 ◽  
Vol 31 (11) ◽  
pp. 1905-1906 ◽  
Author(s):  
T Sun ◽  
Y Lien ◽  
L Mailloux
Keyword(s):  
Diabetes Mellitus ◽  
Renal Failure ◽  
Chronic Renal Failure ◽  
Sodium Dodecyl Sulfate ◽  
Small Molecules ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Electrophoretic Pattern ◽  
Renal Tubules

Abstract A 46-year-old black man with diabetes mellitus and hypertension was hospitalized because of myocardial ischemia and chronic renal failure. The electrophoretogram for protein in urine revealed proteins only in the alpha 1, alpha 2, and beta regions. These protein fractions were identified as small molecules by sodium dodecyl sulfate/polyacrylamide gel electrophoresis. No albumin was detected in the urine. The molecular mass of albumin, the protein present in highest concentration in serum, is near the glomerular filtration threshold, and this protein is not reabsorbed by renal tubules; therefore, albumin is consistently present in proteinuric specimens. Thus this analbuminuric pattern is highly unusual. Although the mechanism of the analbuminuria in this case is not fully understood, we wished to document this extremely rare electrophoretic pattern to alert clinical chemists and pathologists of its existence.

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