scholarly journals Isoenzyme polymorphism of almond genotypes selected in the region of northern Serbia

2010 ◽  
Vol 37 (No. 2) ◽  
pp. 56-61 ◽  
Author(s):  
S. Čolić ◽  
D. Milatović ◽  
D. Nikolić ◽  
G. Zec
Keyword(s):  
Cluster Analysis ◽  
Alkaline Phosphatase ◽  
Gel Electrophoresis ◽  
Malic Enzyme ◽  
Formate Dehydrogenase ◽  
Polyacrylamide Gel Electrophoresis ◽  
Prunus Dulcis ◽  
Enzyme Systems ◽  
Isoenzyme Polymorphism ◽  
First Time

Isoenzyme polymorphism was studied in 20 almond (Prunus dulcis [Mill.] D.A. Webb) genotypes selected from seedling populations of unknown almond cultivars in the region of northern Serbia (Vojvodina). Fourteen enzyme systems were studied using the method of vertical polyacrylamide gel electrophoresis. Ten systems were polymorphic in twelve loci. This polymorphism allowed unique identification of all studied genotypes. The most useful enzyme for analysis of almond genetic variability was menadione reductase. Polymorphism identified for alkaline phosphatase, formate dehydrogenase, glutamate dehydrogenase, malic enzyme, and menadione reductase was reported for the first time in almond. Cluster analysis was used to construct a dendrogram on which five clusters with different number of genotypes could be identified.

Isozyme Variation in Broom Snakeweed (Gutierrezia sarothrae)

Weed Science ◽  
1995 ◽  
Vol 43 (1) ◽  
pp. 156-162 ◽  
Author(s):  
Yanglin Hou ◽  
Tracy M. Sterling
Keyword(s):  
Cluster Analysis ◽  
New Mexico ◽  
Genetic Variability ◽  
Gel Electrophoresis ◽  
Isozyme Analysis ◽  
Starch Gel Electrophoresis ◽  
Enzyme Systems ◽  
Starch Gel ◽  
Morphological Differences ◽  
Gutierrezia Sarothrae

Broom snakeweed, a perennial rangeland shrub, is highly variable morphologically and can grow under a broad range of environmental conditions. In this study, isozyme analysis using starch gel electrophoresis was used to quantify genetic variability within and among New Mexico populations of broom snakeweed. Eight separate populations of broom snakeweed and one population of threadleaf snakeweed as a comparison were investigated. of the 10 enzyme systems examined, 16 loci were identified in eight populations and two species. Eleven loci were monomorphic in eight populations and two species and five loci were polymorphic in at least one population or species. Genetic variability was large in broom and threadleaf snakeweed populations as determined by isozyme analysis. Genetic variability among broom snakeweed populations was greater than that within populations for the five polymorphic loci. Cluster analysis of genetic distance and identity for the eight populations and two species characterized two major groups. Within broom snakeweed, cluster analysis characterized five groups. The two species shared most common alleles. The genetic variation identified in this research may account for the morphological differences and broad geographical distribution of broom snakeweed.

Quantitative Recovery of Alkaline Phosphatase and γ-Glutamyl Transferase Isoenzymes after Polyacrylamide Gel Electrophoresis

1980 ◽  
Vol 17 (1) ◽  
pp. 15-19 ◽  
Author(s):  
TJ Brooks ◽  
HG Sammons
Keyword(s):  
Alkaline Phosphatase ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Glutamyl Transferase ◽  
Quantitative Recovery

Loss of activity of the isoenzymes of γ-glutamyl transferase and alkaline phosphatase has been shown to occur during electrophoresis on polyacrylamide gel. After studying the possible factors concerned in this loss, reasonable recovery from the gel can be obtained only for the isoenzyme staying at the origin. Maximum recovery is 60% for origin γ-glutamyl transferase and 92% for origin alkaline phosphatase.

scholarly journals Allozyme pattern for new record of Craspedacusta sowerbii in Serbia

2004 ◽  
pp. 15-19 ◽  
Author(s):  
Jasmina Ludoski ◽  
Vesna Milankov ◽  
Predrag Radisic
Keyword(s):  
Genetic Variability ◽  
Natural Population ◽  
Gel Electrophoresis ◽  
New Record ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Serbia And Montenegro ◽  
Enzyme Loci ◽  
First Time

Cosmopolitan freshwater jellyfish Craspedacusta sowerbii L a n k e s t e r 1880 (Cnidaria, Hydrozoa) was recorded for the first time in the lake Velika peskara near Zrenjanin (Serbia and Montenegro) in summer 1998. A natural population of C. sowerbii from the lake Velika peskara was analyzed for genetic variability at 9 enzyme loci (Gpi, Hk, Idh-1, Idh-2, Me, Mdh-1 Mdh-2, Pgm and Sod) by polyacrylamide gel electrophoresis. A zymogram indicated that population was monomorphic at all analyzed loci.

A comparison of certain isozyme patterns in lobeless and normal embryos of the snail, Ilyanassa obsoleta

Development ◽  
1971 ◽  
Vol 26 (3) ◽  
pp. 339-349
Author(s):  
Sallie B. Freeman
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Ilyanassa Obsoleta ◽  
Alkaline Phosphatases ◽  
Polar Lobe ◽  
Specific Nature ◽  
Isozyme Patterns

A study was made of the emergence of certain enzymes during the embryogenesis of Ilyanassa. Lobeless and normal embryos were compared in order to determine the effect of polar lobe removal on subsequent molecular developments. Polyacrylamide gel electrophoresis in capillary tubes, a technique requiring only small numbers of embryos, was used to obtain the isozyme patterns of alkaline phosphatases and of esterases. It was found that lobe removal interfered with the emergence of normal isozyme patterns of alkaline phosphatase and esterase during development. Certain bands of enzyme activity were severely reduced or absent while others appeared to be normal. The results provide further evidence that the influence of the polar lobe on development is of a specific nature.

scholarly journals Wheat: A New Natural Host for the Mal De Río Cuarto Virus in the Endemic Disease Area, Río Cuarto, Córdoba Province, Argentina

Plant Disease ◽  
1998 ◽  
Vol 82 (2) ◽  
pp. 149-152 ◽  
Author(s):  
P. E. Rodriguez Pardina ◽  
M. P. Giménez Pecci ◽  
I. G. Laguna ◽  
E. Dagoberto ◽  
G. Truol
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Wheat Crop ◽  
Enzyme Linked Immunosorbent Assay ◽  
Disease Area ◽  
Random Samples ◽  
Delphacodes Kuscheli ◽  
Preferred Species ◽  
First Time ◽  
Das Elisa

The fijivirus known as “Mal de Río Cuarto” that affects corn is endemic to the area of Río Cuarto, Cordoba Province, Argentina. One of the preferred species for the development of its vector, the insect Delphacodes kuscheli Fennah, is wheat. In this area, wheat plants with deformed leaves, spikes and spikelets, shortened internodes, leaves with serrated borders, and sterile spikelets were detected, suggesting the possibility that Mal de Río Cuarto Virus could also be infecting this crop. Samples originating in Río Cuarto, Sampacho, and La Carlota (Córdoba Province) that showed symptoms, were analyzed by double-antibody sandwich enzyme-linked immunosorbent assay (DAS-ELISA), polyacrylamide gel electrophoresis, and electron microscopy, confirming, for the first time, the occurrence of the disease in wheat. The frequency of the disease was assessed in random samples from 14 wheat plots located in the Department of Río Cuarto (Córdoba Province). The samples were analyzed using the DASELISA immunoenzymatic technique, and the disease was detected in the majority of the fields assessed, with levels of incidence that ranged between 2.5 and 24%. We must be aware of the presence of this virus in the wheat crop, where it appears to play a double role in the epidemiology of the disease, acting both as a virus reservoir and as a preferred host for the development of populations of the vector virus, D. kuscheli.

scholarly journals The preparation of monoclonal antibodies to human bone and liver alkaline phosphatase and their use in immunoaffinity purification and in studying these enzymes when present in serum

1987 ◽  
Vol 244 (3) ◽  
pp. 725-733 ◽  
Author(s):  
E M Bailyes ◽  
R N Seabrook ◽  
J Calvin ◽  
G A Maguire ◽  
C P Price ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Cellulose Acetate ◽  
Liver Enzyme ◽  
Gel Electrophoresis ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Bone Alkaline Phosphatase ◽  
Serum Enzyme ◽  
Cellulose Acetate Electrophoresis ◽  
Immunoaffinity Purification

1. Liver and bone alkaline phosphatase isoenzymes were solubilized with the zwitterionic detergent sulphobetaine 14, and purified to homogeneity by using a monoclonal antibody previously raised against a partially-purified preparation of the liver isoenzyme. Both purified isoenzymes had a specific activity in the range 1100-1400 mumol/min per mg of protein with a subunit Mr of 80,000 determined by SDS/polyacrylamide gel electrophoresis. Butanol extraction instead of detergent solubilization, before immunoaffinity purification of the liver enzyme, resulted in the same specific activity and subunit Mr. The native Mr of the sulphobetaine 14-solubilized enzyme was consistent with the enzyme being a dimer of two identical subunits and was higher than that of the butanol-extracted enzyme, presumably due to the binding of the detergent micelle. 2. Pure bone and liver alkaline phosphatase were used to raise further antibodies to the two isoenzymes. Altogether, 27 antibody-producing cell lines were cloned from 12 mice. Several of these antibodies showed a greater than 2-fold preference for bone alkaline phosphatase in the binding assay used for screening. No antibodies showing a preference for liver alkaline phosphatase were successfully cloned. None of the antibodies showed significant cross-reaction with placental or intestinal alkaline phosphatase. Epitope analysis of the 27 antibodies using liver alkaline phosphatase as antigen gave rise to six groupings, with four antibodies unclassified. The six major epitope groups were also observed using bone alkaline phosphatase as antigen. 3. Serum from patients with cholestasis contains soluble and particulate forms of alkaline phosphatase. The soluble serum enzyme had the same size and charge as butanol-extracted liver enzyme on native polyacrylamide-gel electrophoresis. Cellulose acetate electrophoresis separated the soluble and particulate serum alkaline phosphatases as slow- and fast-moving forms respectively. In the presence of sulphobetaine 14 all the serum enzyme migrated as the slow-moving form on cellulose acetate electrophoresis. Monoclonal anti-(alkaline phosphatase) immunoadsorbents did not bind the particulate form of alkaline phosphatase in cholestatic serum but bound the soluble form. In the presence of sulphobetaine 14 all the cholestatic serum alkaline phosphatase bound to the immunoadsorbents. 4. The electrophoretic and immunological data are consistent with both particulate and soluble forms of alkaline phosphatase in cholestatic serum being derived from the hepatocyte membrane.

Electrophoretic Separation of Alkaline Phosphatase Isoenzymes: A Clinical Evaluation

1972 ◽  
Vol 17 (5) ◽  
pp. 172-175 ◽  
Author(s):  
R. R. G. Warwick ◽  
D. J. C. Shearman ◽  
I. W. Percy-Robb ◽  
A. F. Smith
Keyword(s):  
Alkaline Phosphatase ◽  
Gel Electrophoresis ◽  
Serum Alkaline Phosphatase ◽  
Polyacrylamide Gel Electrophoresis ◽  
Total Serum ◽  
Electrophoretic Separation ◽  
Nucleotidase Activity ◽  
Total Alkaline Phosphatase ◽  
Alkaline Phosphatase Isoenzymes ◽  
Total Alkaline

In 40 patients with a raised total serum alkaline phosphatase, polyacrylamide gel electrophoresis was used to separate the liver, bone and intestinal isoenzymes of alkaline phosphatase. The method confirmed the source of the raised alkaline phosphatase in patients with established bone or liver disease. The technique was found to be more reliable than the estimation of 5'-nucleotidase activity in the detection of a raised alkaline phosphatase of hepatic origin and was also useful when the raised total alkaline phosphatase came from two sources.

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