scholarly journals PAG electrophoregrams of six Finnish potato cultivars

1985 ◽  
Vol 57 (3) ◽  
pp. 147-154
Author(s):  
Tuula Sontag ◽  
Hannu Salovaara ◽  
Osmo Ulvinen
Keyword(s):  
Soluble Protein ◽  
Protein Separation ◽  
Electrophoretic Pattern ◽  
Soluble Proteins ◽  
Polyacrylamide Gel ◽  
Potato Cultivars ◽  
Good Resolution ◽  
Local Cultivars ◽  
Close Relatives

The polyacrylamide gel electrophoretic (PAGE) patterns of soluble proteins and esterases of six Finnish potato cultivars (Jaakko, Pito, Hankkijan Timo, Hankkijan Tuomas, Hankkijan Tanu and Puikula) were determined. All cultivars are commonly grown in Finland. The PAGE procedure used yielded highly reproducible protein separation and good resolution. Samples studied had specific soluble protein and esterase PAGE patterns, indicating that electrophoregrams can be used for identifying Finnish potato cultivars. Only two cultivars, Hankkijan Tanu and Hankkijan Tuomas, which are close relatives, possessed very similar PAGE patterns. The electrophoretic pattern of Puikula was very similar to that of the Swedish cultivar Mandel when compared with the reference presented in the literature.Therefore a hypothesis is presented suggesting that these two local cultivars would be representatives of the same cultivar.

Relation of age of cultures to yield of mycelium, hydrogen cyanide production, peroxidases, and proteins from mycelium of a low-temperature basidiomycete

1968 ◽  
Vol 14 (11) ◽  
pp. 1169-1172 ◽  
Author(s):  
Awatar S. Sekhon ◽  
Nicholas Colotelo
Keyword(s):  
Low Temperature ◽  
Hydrogen Cyanide ◽  
Soluble Protein ◽  
Dry Weight ◽  
Soluble Proteins ◽  
Polyacrylamide Gel

Changes in dry weight, hydrogen cyanide production, peroxidase, and soluble proteins of mycelium of a low-temperature basidiomycete with age of cultures were studied.Hydrogen cyanide was detected only after there was a decrease in growth of mycelium as determined by dry-weight measurements. Polyacrylamide gel electrophoretic analyses showed that the pattern and numbers of peroxidase and other soluble-protein bands varied with the age of the culture. Concomitant with decreases in yield of mycelium, there was a decrease in the numbers of peroxidase and soluble-protein bands.

Isoelectric focusing of soluble proteins in the characterization of three species of Hymenolepis (Cestoda)

1985 ◽  
Vol 63 (7) ◽  
pp. 1720-1723 ◽  
Author(s):  
Brent R. Dixon ◽  
Hisao P. Arai
Keyword(s):  
Isoelectric Focusing ◽  
Protein Separation ◽  
Soluble Proteins ◽  
Hymenolepis Diminuta ◽  
Good Resolution ◽  
Banding Patterns ◽  
Morphological Approach ◽  
Single Host ◽  
Taxonomic Studies

A technique involving protein separation was used as an alternative to a morphological approach in the differentiation of the tapeworms Hymenolepis diminuta, H. citelli, and H. microstoma. Isoelectric focusing of soluble proteins was performed on Polyacrylamide gels using extracts from whole, adult worms. Each species of Hymenolepis was found to have a unique protein banding pattern, although some bands appeared to be common to two or all three species. Very little difference was found in the protein banding patterns of worms of a given species, whether they were from a single host individual or two different host individuals of the same species. There was also little difference between gels in the banding patterns of a given species. This technique of soluble protein isoelectric focusing is simple and reproducible, has very good resolution, and seems well suited to taxonomic studies involving tapeworms.

An investigation of host influence on soluble protein banding profiles of Hymenolepis spp. (Cestoidea), using isoelectric focusing

1987 ◽  
Vol 65 (10) ◽  
pp. 2471-2474 ◽  
Author(s):  
Brent R. Dixon ◽  
Hisao P. Arai
Keyword(s):  
Isoelectric Focusing ◽  
Definitive Host ◽  
Host Species ◽  
Soluble Protein ◽  
Protein Separation ◽  
Soluble Proteins ◽  
Banding Patterns ◽  
Morphological Approach ◽  
Alternative Means ◽  
Host Influence

Protein separation techniques have been utilized in recent years as alternative means of differentiating species and strains of tapeworms. As with the traditional morphological approach, however, there is the potential for host influence. For such separative techniques to be useful taxonomically it is important that the banding profiles differentiating parasites be consistent, regardless of host species. To test for host influence, two Hymenolepis species were maintained both in preferred and alternative definitive host species. The soluble proteins of tapeworms of a given species, from the different host species, were then subjected to isoelectric focusing, and the resulting banding patterns were compared. There were no noticeable differences in the banding profiles of these worms, indicating a lack of host influence. If these findings hold for other tapeworm genera, isoelectric focusing of soluble proteins could have practical value in parasite surveys.

Quantitation of Beta Lipoprotein (LDL) Cholesterol by Densitometric Evaluation of Disc Electropherograms

1972 ◽  
Vol 18 (3) ◽  
pp. 217-221 ◽  
Author(s):  
Robert F Moran ◽  
William P Castelli ◽  
Marianne V Moran
Keyword(s):  
Ldl Cholesterol ◽  
Electrophoretic Pattern ◽  
Disc Electrophoresis ◽  
Polyacrylamide Gel ◽  
Type Ii ◽  
Chemical Concentration ◽  
Type Iv ◽  
Chemical Technique ◽  
Peak Areas

Abstract This paper describes a rapid, facile, and accurate new procedure for determination of marginal Type IV or Type II hyperlipoproteinemias, in which discontinuous (disc) electrophoresis on polyacrylamide gel is used to quantitate LDL (beta) cholesterol without ultracentrifugation. Fasting sera, previously assayed by ultracentrifugation and chemical technique, were prestained with Sudan Black, and the lipoproteins were separated by disc electrophoresis. The beta-lipoprotein fraction of each electrophoretic pattern was quantitated by densitometry. The values for the integrated densitometric peak areas for the beta fraction and the chemically assayed cholesterol of the ultracentrifuged LDL fraction correlated well (r = .90). Results were determined from a curve relating chemical concentration of the integrated peak values by densitometry to the known LDL cholesterol of a series of standards.

A New Method for Proteome Screening with Two-Dimensional Urea-Sds Polyacrylamide Gel Electrophoresis

2014 ◽  
Vol 1 (1) ◽  
Author(s):  
Areeba Ahmad ◽  
Riaz Ahmad
Keyword(s):  
Gel Electrophoresis ◽  
Protein Separation ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Cost Effective ◽  
Polyacrylamide Gel ◽  
Present System ◽  
Liver Protein ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis

AbstractTwo-dimensional gel electrophoresis (2DE) separating proteins on the basis of their pI and molecular mass remain the best available technique for protein separation and characterization to date. But due to several limitations, including streak formation in IEF gels, partial solubility of proteins, expensive running conditions and relatively longer time taken, a simple urea-SDS-2D polyacrylamide gel electrophoresis (US2DE) is described here. The system is reasonably sensitive, cost effective with good reproducibility. The method described in this paper employs a chaotropic agent, urea, in the first dimension and sodium dodecyl sulphate (SDS), like conventional system, in the second dimension with an addition of polyacrylamide to screen the liver proteome of healthy and chemically induced fibrotic rats. The system separates the protein on the basis of chargeto- mass ratio and clearly demonstrates differential expression in the liver protein repertoire of healthy and fibrotic rats. Moreover, the present system, like other 2D electrophoretic procedures revealed at least 22 novel spots in the investigated tissues. The technique may be utilized for comprehensive proteome screening of any biological sample and would provide an overview to narrow down the candidate proteins or biomarkers.

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