Larval Insect Identification by Cellulose Acetate Gel Electrophoresis and Its Application to Life History Evaluation and Cohort Analysis

1993 ◽  
Vol 12 (3) ◽  
pp. 270-278 ◽  
Author(s):  
Jacek Zloty ◽  
Gordon Pritchard ◽  
Rangathilakam Krishnaraj
Keyword(s):  
Life History ◽  
Cellulose Acetate ◽  
Gel Electrophoresis ◽  
Cohort Analysis ◽  
Insect Identification ◽  
Larval Insect

scholarly journals Clonal variation within a mucosal isolate derived from a patient with Leishmania (Viannia) braziliensis infection

1991 ◽  
Vol 33 (5) ◽  
pp. 343-350 ◽  
Author(s):  
César Augusto Cuba-Cuba ◽  
David Evans ◽  
Ana de Cassia Rosa ◽  
Philip Davis Marsden
Keyword(s):  
Monoclonal Antibodies ◽  
Cellulose Acetate ◽  
Phenotypic Variation ◽  
Gel Electrophoresis ◽  
Clonal Variation ◽  
Starch Gel Electrophoresis ◽  
Mucosal Leishmaniasis ◽  
Starch Gel

Three isolates over 5 years from a patient with persistent relapsing mucosal leishmaniasis due to Leishmania (Viannia) braziliensis and 7 clones from one of these isolates were studied by zymodemes and scrodemes analysis. Results showed evidences of clonal phenotypic variation. Eight isoenzymes markers demonstrated clear differences on Cellulose Acetate (CA) and thin starch gel electrophoresis. Also a panel of specific monoclonal antibodies showed such differences. Our observations provide additional evidence that Leishmania (Viannia) braziliensis is composed by subpopulations of parasites with peculiar biochemical and antigenic characteristics.

scholarly journals Estructura genética de poblaciones de Eriocaulon bilobatum (Eriocaulaceae): una especie amenazada de humedades temporales

2019 ◽  
Vol 85 ◽  
pp. 81
Author(s):  
Fabiola Magallán Hernández ◽  
Mahinda Martínez ◽  
Luis Hernández Sandoval ◽  
Ken Oyama
Keyword(s):  
Genetic Diversity ◽  
Life History ◽  
Genetic Structure ◽  
Gel Electrophoresis ◽  
Life History Traits ◽  
Aquatic Environments ◽  
Starch Gel Electrophoresis ◽  
Temporary Wetlands ◽  
Sexual And Asexual Reproduction ◽  
Starch Gel

<em>Eriocaulon bilobatum</em> is an aquatic species that inhabits temporary wetlands in central Mexico. It is annual, herbaceous, emergent, with sexual and asexual reproduction, monoecious and insect pollinated. It is a rare and vulnerable species due to its endangered habitats. The objectives of this study were to determine the diversity and genetic structure of <em>E. bilobatum </em> and to know if there is a correlation with genetic diversity and its ecological and life history traits. Using horizontal starch-gel electrophoresis, we screened 160 individuals from four populations. <em>E. bilobatum</em> has a higher genetic diversity (A=2.32, Ae=1.31, P=69.65, Ho=0.134, He=0.197, HT=0.221) than species with similar ecological and life history traits, moderate levels of inbreeding (FIS = 0.312) and low genetic differentiation among populations (FST = 0.053 y GST = 0.048). Its diversity and genetic structure are determined by the mating system and life history traits, more than by inhabiting aquatic environments.

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.

scholarly journals Improved Measurement of Monoclonal Paraproteins in Serum Using Agarose Gel Electrophoresis

1987 ◽  
Vol 24 (1) ◽  
pp. 73-76 ◽  
Author(s):  
P M Dennis ◽  
B Biegler ◽  
R Papas
Keyword(s):  
Cellulose Acetate ◽  
Gel Electrophoresis ◽  
Brilliant Blue ◽  
Agarose Gel ◽  
Agarose Gel Electrophoresis ◽  
Brilliant Blue G ◽  
Cellulose Acetate Electrophoresis ◽  
Coomassie Brilliant Blue ◽  
Ponceau S ◽  
Coomassie Brilliant

Serum paraproteins can be accurately and precisely measured by means of agarose gel electrophoresis and densitometry at 520 nm after staining with Coomassie Brilliant Blue G. The results obtained for this method agree closely with the quantity of paraprotein recoverable from preparative agarose gel electrophoresis. The method is preferable to cellulose acetate electrophoresis stained with Ponceau S.

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