scholarly journals Characterization of Pyrus Species and Cultivars Using Gradient Polyacrylamide Gel Electrophoresis

1986 ◽  
Vol 4 (2) ◽  
pp. 56-60
Author(s):  
R.A. Menendez ◽  
L.S. Daley
Keyword(s):  
Acid Phosphatase ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Growing Season ◽  
Chemical Identification ◽  
Identification Procedure ◽  
Genetic Characteristics ◽  
Isozyme Patterns ◽  
Anionic Polyacrylamide

A chemical identification procedure previously used to identify apple clones was tried with pear species and clones. Following electrophoresis, the peroxidase, esterase, and acid phosphatase isozyme patterns on anionic polyacrylamide gradient gels were determined. These patterns were found to vary with the species and clone, but not to change, within a clone during the growing season. Thus, these patterns were considered to represent genetic characteristics. The patterns were used to identify 37 selected Pyrus accessions at the National Clonal Germplasm Repository, Corvallis, Oregon. All species tested were distinguishable using this system. All the accessions of P. calleryana selected from the NCGR collection were distinct: however, one clone from outside the collection had an identical pattern to one inside the collection. Among the Chinese pear clones (complex hybrids of P. ussuriensis × P. pyrifolia) tested, three pairs of clones had the same combination. This technique appears to have the potential to readily identify pear specimens, and could be an important aid in the characterization of germplasm material.

scholarly journals Characterization of Filbert (Corylus) Species and Cultivars Using Gradient Polyacrylamide Gel Electrophoresis

1987 ◽  
Vol 5 (1) ◽  
pp. 11-16
Author(s):  
Z. Ahmad ◽  
L.S. Daley ◽  
R.A. Menendez ◽  
H.B. Lagerstedt
Keyword(s):  
Acid Phosphatase ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Phenol Oxidase ◽  
Chemical Identification ◽  
Identification Procedure ◽  
Genetic Characteristics ◽  
Isozyme Patterns ◽  
Anionic Polyacrylamide

A chemical identification procedure previously used to identify apple and pear species, cultivars and clonal accessions, was tried with Corylus (filbert, hazel) species, cultivars and clonal accessions. Following electrophoresis, the peroxidase, phenol oxidase, and acid phosphatase isozyme patterns on anionic polyacrylamide gradient gels were determined. These patterns were found to vary between clonal accessions, but did not change, within a given accession during and following the test period (May through October). Thus, these patterns were considered to represent genetic characteristics suitable for identification purposes. The patterns were used to identify 78 Corylus accessions at the National Clonal Germplasm Repository Corvallis, Oregon. All accessions tested (species, cultivars and clones) were distinguishable using this system. The diversity of isozyme patterns was greater in Corylus than Pyrus populations previously sampled. This technique appears to have the potential to readily identify filbert accessions and could be an important aid in the characterization of germplasm material.

scholarly journals Characterization of Quince (Cydonia) Cultivars Using Polyacrylamide Gel Electrophoresis

1988 ◽  
Vol 6 (2) ◽  
pp. 53-59 ◽  
Author(s):  
E.E. Sanchez ◽  
R.A. Menendez ◽  
L.S. Daley ◽  
R.B. Boone ◽  
O.L. Jahn ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Phenol Oxidase ◽  
Cydonia Oblonga ◽  
Genetic Characteristics ◽  
Isozyme Patterns ◽  
Gradient Electrophoresis ◽  
Apple Cultivars ◽  
Anionic Polyacrylamide

An investigation of available Cydonia (Cydonia oblonga Mill., quince, membrillo) germplasm by isozyme staining of anionic polyacrylamide gradient electrophoresis gels is described. The isozymes of acid phosphatase, esterase, peroxidase and phenol oxidase showed most diversity and usefulness for this purpose. Eleven groups of quince and two groups of x Pyronia (quince-pear crosses) were distinguished by their isozyme patterns. These patterns distinguish between groups of clonal accessions, and the patterns were constant for each accession during the test period (December, 1986 to August, 1987). Thus, these patterns were considered to represent genetic characteristics suitable for identification purposes. The diversity of isozyme patterns was much less than in Corylus and Pyrus populations previously sampled; and less than that of a restricted pool of apple cultivars previously examined.

Prothrombin Metz : Purification and Characterization of a Variant of Human Prothrombin

1979 ◽  
Author(s):  
M Ribieto ◽  
J Elion ◽  
D Labie ◽  
F Josso
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Factor Xa ◽  
Polyacrylamide Gel ◽  
Cleavage Pattern ◽  
Purification And Characterization ◽  
Double Immunodiffusion ◽  
The Family

For the purification of the abnormal prothrombin (Pt Metz), advantage has been taken of the existence in the family of three siblings who, being double heterozygotes for Pt Metz and a hypoprothrombinemia, have no normal Pt. Purification procedures included barium citrate adsorption and chromatography on DEAE Sephadex as for normal Pt. As opposed to some other variants (Pt Barcelona and Madrid), Pt Metz elutes as a single symetrical peak. By SDS polyacrylamide gel electrophoresis, this material is homogeneous and appears to have the same molecular weight as normal Pt. Comigration of normal and abnormal Pt in the absence of SDS, shows a double band suggesting an abnormal charge for the variant. Pt Metz exhibits an identity reaction with the control by double immunodiffusion. Upon activation by factor Xa, Pt Metz can generate amydolytic activity on Bz-Phe-Val-Arg-pNa (S2160), but only a very low clotting activity. Clear abnormalities are observed in the cleavage pattern of Pt Metz when monitored by SDS gel electrophoresis. The main feature are the accumulation of prethrombin l (Pl) and the appearance of abnormal intermediates migrating faster than Pl.

scholarly journals Characterization of [3H]palmitate- and [3H]ethanolamine-labelled proteins in the multicellular parasitic trematode Schistosoma mansoni

1988 ◽  
Vol 254 (2) ◽  
pp. 419-426 ◽  
Author(s):  
P M Wiest ◽  
E J Tisdale ◽  
W L Roberts ◽  
T L Rosenberry ◽  
A A F Mahmoud ◽  
...  
Keyword(s):  
Schistosoma Mansoni ◽  
Molecular Mass ◽  
Gel Electrophoresis ◽  
Free Amino ◽  
Protein Modification ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Reductive Methylation ◽  
Amide Linkage

Biosynthetic labelling experiments with cercariae and schistosomula of the multicellular parasitic trematode Schistosoma mansoni were performed to determine whether [3H]palmitate or [3H]ethanolamine was incorporated into proteins. Parasites incorporated [3H]palmitate into numerous proteins, as judged by SDS/polyacrylamide-gel electrophoresis and fluorography. The radiolabel was resistant to extraction with chloroform, but sensitive to alkaline hydrolysis, indicating the presence of an ester bond. Further investigation of the major 22 kDa [3H]palmitate-labelled species showed that the label could be recovered in a Pronase fragment which bound detergent and had an apparent molecular mass of 1200 Da as determined by gel filtration on Sephadex LH-20. Schistosomula incubated with [3H]ethanolamine for up to 24 h incorporated this precursor into several proteins; labelled Pronase fragments recovered from the three most intensely labelled proteins were hydrophilic and had a molecular mass of approx. 200 Da. Furthermore, reductive methylation of such fragments showed that the [3H]ethanolamine bears a free amino group, indicating the lack of an amide linkage. We also evaluated the effect of phosphatidylinositol-specific phospholipase C from Staphylococcus aureus: [3H]palmitate-labelled proteins of schistosomula and surface-iodinated proteins were resistant to hydrolysis with this enzyme. In conclusion, [3H]palmitate and [3H]ethanolamine are incorporated into distinct proteins of cercariae and schistosomula which do not bear glycophospholipid anchors. The [3H]ethanolamine-labelled proteins represent a novel variety of protein modification.

Characterization of immunoreactive proteins of Setaria cervi isolated by preparative polyacrylamide gel electrophoresis

2017 ◽  
Vol 62 (1) ◽  
Author(s):  
Priyanka Priyadarshi ◽  
Piyush Dravid ◽  
Inayat Hussain Sheikh ◽  
Sunita Saxena ◽  
Ashish Tandon ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Complex Mixtures ◽  
Setaria Cervi ◽  
Antigenic Proteins ◽  
Specific Antigens

AbstractFilarial parasites are complex mixtures of antigenic proteins and characterization of these antigenic molecules is essential to identify the diagnostically important filaria-specific antigens. In the present study, we have fractionated the somatic extracts from adults of

scholarly journals Purification and characterization of acid phosphatase from a germinating black gram (Vigna mungo L.) seedling

2011 ◽  
Vol 63 (3) ◽  
pp. 747-756 ◽  
Author(s):  
A.K.M. Asaduzzaman ◽  
Habibur Rahman ◽  
Tanzima Yeasmin
Keyword(s):  
Acid Phosphatase ◽  
Gel Electrophoresis ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Inhibitory Effect ◽  
Maximum Activity ◽  
Exchange Chromatography ◽  
Black Gram ◽  
Km Value

An acid phosphatase has been isolated and purified from an extract of a germinating black gram seedling. The method was accomplished by gel filtration of a germinating black gram seedling crude extract on sephadex G-75 followed by ion exchange chromatography on DEAE cellulose. The acid phosphatase gave a single band on SDS-polyacrylamide slab gel electrophoresis. The molecular weight of the acid phosphatase determined by SDS-polyacrylamide slab gel electrophoresis was estimated to be 25 kDa. The purified enzyme showed maximum activity at pH 5 and at temperature of 55?C. Mg2+, Zn2+ and EDTA had an inhibitory effect on the activity of the acid phosphatase. Black gram seedling acid phosphatase was activated by K+, Cu2+ and Ba2+. The Km value of the enzyme was found to be 0.49 mM for pNPP as substrate.

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