Heterogeneity of antifreeze polypeptides from the Newfoundland winter flounder, Pseudopleuronectes americanus

1984 ◽  
Vol 62 (1) ◽  
pp. 28-33 ◽  
Author(s):  
Ron M. Fourney ◽  
Shashikant B. Joshi ◽  
Ming H. Kao ◽  
Choy L. Hew
Keyword(s):  
Molecular Weight ◽  
High Performance Liquid Chromatography ◽  
Gel Electrophoresis ◽  
High Performance ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Winter Flounder ◽  
Pseudopleuronectes Americanus ◽  
Reverse Phase ◽  
Antifreeze Polypeptides

The heterogeneity of Newfoundland winter flounder antifreeze polypeptides was analyzed by reverse phase high performance liquid chromatography and by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Seven antifreeze polypeptide components could be readily demonstrated. Five of the components were similar in molecular weight (3300) and amino acid composition. Two of the antifreeze polypeptide components were larger (4500) and contained valine. The two major components (components 6 and 8) were identical to those reported earlier from our laboratories.

A glyco-phosphoprotein in human milk

1987 ◽  
Vol 54 (2) ◽  
pp. 199-205 ◽  
Author(s):  
Norihiro Azuma ◽  
Kunio Yamauchi
Keyword(s):  
Molecular Weight ◽  
High Performance Liquid Chromatography ◽  
Liquid Chromatography ◽  
Gel Electrophoresis ◽  
High Performance ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Sedimentation Coefficient ◽  
Reversed Phase ◽  
Ultracentrifugal Analysis

SummaryA highly glycosylated phosphoprotein (HGPP) was isolated from a human casein fraction by reversed-phase high-performance liquid chromatography. This component contained carbohydrates to ∼ 38·2% (w/w) and phosphorus to ∼ 1·6% (w/w). The molecular weight of this HGPP as estimated by sodium dodecyl sulphate–polyacrylamide gel electrophoresis ∼ 41000. Ultracentrifugal analysis revealed that the sedimentation coefficient of the HGPP was 2·6S in a 10 mM-imidazole-HCl buffer at pH 7·0 and 27 °C, but this component interacted with human κ-casein and formed a complex with s = 10·4S.

scholarly journals Genotypic Transitions among Bluetongue Viral Isolates from Domestic Ruminants in Colorado during 1981–1984

1989 ◽  
Vol 1 (3) ◽  
pp. 242-246
Author(s):  
Ellen W. Collisson ◽  
T. Lynwood Barber ◽  
Colleen M. Shannon ◽  
Maurice C. Kemp
Keyword(s):  
Gel Electrophoresis ◽  
Bluetongue Virus ◽  
High Performance ◽  
Viral Infections ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Reverse Phase ◽  
Domestic Ruminants ◽  
The Us ◽  
Viral Isolates

Two predominant electropherotypes of bluetongue virus (BTV) serotype 11 isolates from cattle during a 1981–1984 field study in eastern Colorado were characterized. The genomes of strains isolated from the first 2 years of the study had 1 predominant electropherotype (CO81), with the exception of 1 isolate that differed only in the migration of segment 3. A second electropherotype (CO83), with differences in the migration of 4 segments, coexisted in the same region during 1983 and 1984 with strains having the CO81 RNA profile. The genomes of CO81 and CO83 were also distinguishable from those of the US prototype of BTV 11. Analysis of the polypeptides of representative strains of each electropherotype by sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicated that the proteins were very similar. The occurrence of the CO81 electropherotype was apparently the result of multiple viral infections since the positions of 7 segments had faint second bands and single-banded variants were isolated after serial plaque purifications. In addition, protein 7 of 1 of the CO81 isolates and protein 7 of the single-banded variant differed as shown by reverse phase-high performance liquid chromatography of 35S-methionine-labeled tryptic peptides.

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