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.

An investigation of host influence on soluble protein banding profiles of Hymenolepis spp. (Cestoidea), using isoelectric focusing

1987 ◽  
Vol 65 (10) ◽  
pp. 2471-2474 ◽  
Author(s):  
Brent R. Dixon ◽  
Hisao P. Arai
Keyword(s):  
Isoelectric Focusing ◽  
Definitive Host ◽  
Host Species ◽  
Soluble Protein ◽  
Protein Separation ◽  
Soluble Proteins ◽  
Banding Patterns ◽  
Morphological Approach ◽  
Alternative Means ◽  
Host Influence

Protein separation techniques have been utilized in recent years as alternative means of differentiating species and strains of tapeworms. As with the traditional morphological approach, however, there is the potential for host influence. For such separative techniques to be useful taxonomically it is important that the banding profiles differentiating parasites be consistent, regardless of host species. To test for host influence, two Hymenolepis species were maintained both in preferred and alternative definitive host species. The soluble proteins of tapeworms of a given species, from the different host species, were then subjected to isoelectric focusing, and the resulting banding patterns were compared. There were no noticeable differences in the banding profiles of these worms, indicating a lack of host influence. If these findings hold for other tapeworm genera, isoelectric focusing of soluble proteins could have practical value in parasite surveys.

Characterization of Hymenolepis diminuta (Cestoidea) strains, using enzyme isoelectric focusing

1991 ◽  
Vol 69 (4) ◽  
pp. 1130-1132 ◽  
Author(s):  
Brent R. Dixon ◽  
Hisao P. Arai
Keyword(s):  
Isoelectric Focusing ◽  
Malic Enzyme ◽  
Hymenolepis Diminuta ◽  
Wild Type ◽  
Japanese Strain ◽  
Banding Patterns ◽  
Agarose Gels ◽  
Enzyme Pattern ◽  
Polymorphic Nature

This study evaluates the use of enzyme isoelectric focusing on thin-layer agarose gels in the differentiation of six geographical isolates of the rat tapeworm Hymenolepis diminuta. Differences in the enzyme profiles among these strains were apparent in two of five enzymes examined. A Japanese strain differed from all others in its more anodally positioned malic enzyme bands. This enzyme profile may be attributed to its more recent isolation from the wild type or to the unique origin of this strain. Two qualitatively different phosphoglucomutase banding patterns were apparent among the H. diminuta strains. This polymorphic nature of phosphoglucomutase has similarly been observed in a number of earlier studies. A number of problems are associated with the traditional morphological means of identifying cestodes, particularly at the intraspecific level. The enzyme pattern differences observed among the strains in this study indicate that enzyme isoelectric focusing may be a useful alternative.

scholarly journals Characterization of adult Dicrocoelium dendriticum by isoelectric focusing

1998 ◽  
Vol 72 (2) ◽  
pp. 109-116 ◽  
Author(s):  
R. Campo ◽  
M.Y. Manga-González ◽  
C. González-Lanza ◽  
D. Rollinson ◽  
H. Sandoval
Keyword(s):  
Isoelectric Focusing ◽  
Small Area ◽  
Water Soluble ◽  
North West ◽  
Dicrocoelium Dendriticum ◽  
Glycerophosphate Dehydrogenase ◽  
Glucose Phosphate ◽  
Single Host ◽  
Ph Range

AbstractWater soluble extracts of 3131 adult specimens of Dicrocoelium dendriticum from cattle, sheep and goats, mainly from León province, were analysed by isoelectric focusing in thin-layer polyacrylamide gels. Activity of the following enzymes was studied: lactate dehydrogenase (LDH, EC 1.1.1.27), glucose phosphate isomerase (GPI, EC 5.3.1.9), phosphoglucomutase (PGM, EC 2.7.5.1), acid phosphatase (AcP, EC 3.1.3.2), α-glycerophosphate dehydrogenase (α-GPDH, EC 1.1.1.8), hydroxybutyrate dehydrogenase (HBDH, EC 1.1.1.30) and malate dehydrogenase (MDH, 1.1.1.37). Five distinct enzyme types were recognized for LDH (pH range 6.30–7.13), GPI (pH 6.13–6.80) and PGM (pH 6.20–6.60) whereas AcP showed three different patterns (pH 5.70–5.92). Weak and diffuse activity was detected for MDH (pH 4.8–6.2) and no activity was observed for α-GPDH and HBDH. In general, little phenotypic variation was observed between worms recovered from a single host, between those from hosts of the same species and between those from hosts of different species, although some enzyme types were found in some animals but not others. Nevertheless, it must be taken into account that most parasites came from sheep and also from a relatively small area in north-west Spain.

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

scholarly journals PAG electrophoregrams of six Finnish potato cultivars

1985 ◽  
Vol 57 (3) ◽  
pp. 147-154
Author(s):  
Tuula Sontag ◽  
Hannu Salovaara ◽  
Osmo Ulvinen
Keyword(s):  
Soluble Protein ◽  
Protein Separation ◽  
Electrophoretic Pattern ◽  
Soluble Proteins ◽  
Polyacrylamide Gel ◽  
Potato Cultivars ◽  
Good Resolution ◽  
Local Cultivars ◽  
Close Relatives

The polyacrylamide gel electrophoretic (PAGE) patterns of soluble proteins and esterases of six Finnish potato cultivars (Jaakko, Pito, Hankkijan Timo, Hankkijan Tuomas, Hankkijan Tanu and Puikula) were determined. All cultivars are commonly grown in Finland. The PAGE procedure used yielded highly reproducible protein separation and good resolution. Samples studied had specific soluble protein and esterase PAGE patterns, indicating that electrophoregrams can be used for identifying Finnish potato cultivars. Only two cultivars, Hankkijan Tanu and Hankkijan Tuomas, which are close relatives, possessed very similar PAGE patterns. The electrophoretic pattern of Puikula was very similar to that of the Swedish cultivar Mandel when compared with the reference presented in the literature.Therefore a hypothesis is presented suggesting that these two local cultivars would be representatives of the same cultivar.

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
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