scholarly journals Isoelectric Focusing of Soluble Proteins in the Characterization of Species and Isolates of Nematodirus (Nematoda: Trichostrongyloidea)

1997 ◽  
Vol 83 (5) ◽  
pp. 895 ◽  
Author(s):  
Lora G. Rickard ◽  
Eric P. Hoberg ◽  
Donna M. Mulrooney ◽  
Gary L. Zimmerman
Keyword(s):  
Isoelectric Focusing ◽  
Soluble Proteins

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.

scholarly journals Carbohydrate binding activities of Bradyrhizobium japonicum. II. Isolation and characterization of a galactose-specific lectin.

1990 ◽  
Vol 111 (4) ◽  
pp. 1639-1643 ◽  
Author(s):  
S C Ho ◽  
M Schindler ◽  
J L Wang
Keyword(s):  
Isoelectric Focusing ◽  
Bradyrhizobium Japonicum ◽  
Affinity Column ◽  
Carbohydrate Binding ◽  
Binding Affinities ◽  
Isolation And Characterization ◽  
Relative Binding ◽  
Mannose Derivatives ◽  
Derivatives Of

Extracts of Bradyrhizobium japonicum were fractionated on Sepharose columns covalently derivatized with lactose. Elution of the material that was specifically bound to the affinity column with lactose yielded a protein of Mr approximately 38,000. Isoelectric focusing of this sample yielded two spots with pI values of 6.4 and 6.8. This protein specifically bound to galactose-containing glycoconjugates, but did not bind either to glucose or mannose. Derivatives of galactose at the C-2 position showed much weaker binding; there was an 18-fold difference in the relative binding affinities of galactose versus N-acetyl-D-galactosamine. These results indicate that we have purified a newly identified carbohydrate-binding protein from Bradyrhizobium japonicum, that can exquisitely distinguish galactose from its derivatives at the C-2 position.

Characterization of free and tightly bound lipoprotein in intima by thin layer isoelectric focusing

1979 ◽  
Vol 33 (3) ◽  
pp. 329-342 ◽  
Author(s):  
Elspeth B. Smith ◽  
Heather S. Dietz ◽  
Isobel B. Craig
Keyword(s):  
Thin Layer ◽  
Isoelectric Focusing

Capillary isoelectric focusing (CIEF) for the characterization of humic substances

1997 ◽  
Vol 31 (8) ◽  
pp. 2037-2049 ◽  
Author(s):  
Ph. Schmitt ◽  
A.W. Garrison ◽  
D. Freitag ◽  
A. Kettrup
Keyword(s):  
Humic Substances ◽  
Isoelectric Focusing ◽  
Capillary Isoelectric Focusing

scholarly journals Studies on the heparin sulphamidase activity from rat spleen. Intracellular distribution and characterization of the enzyme

1974 ◽  
Vol 139 (3) ◽  
pp. 699-708 ◽  
Author(s):  
Yochanan Friedman ◽  
Charalampos Arsenis
Keyword(s):  
Isoelectric Focusing ◽  
Intracellular Distribution ◽  
Distinct Entity ◽  
Lysosomal Fraction

A sulphamidase activity present in rat spleen capable of hydrolysing N-[35S]sulphated heparin was studied. This activity was associated with the lysosomal fraction. Studies in vivo showed that the rat is capable of significantly desulphating heparin. Lysosomes in all the major tissues can effectively accumulate heparin. The heparin sulphamidase and arylsulphatase activities from rat spleen were separated by isoelectric focusing. Heparin sulphamidase was a distinct entity from all the arylsulphatase activities.

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