Isozyme characterization of 28 cell lines from five insect species

1985 ◽  
Vol 63 (10) ◽  
pp. 2270-2276 ◽  
Author(s):  
G. T. Harvey ◽  
S. S. Sohi

Correct identity of cell lines is essential for their use in any investigation; isozyme patterns of cell cultures can give reliable identification. Starch gel electrophoresis was used to develop isozyme profiles of 8 hymenopteran and 20 lepidopteran cell lines and of the insect species from which they were developed. Species identity of 26 of the cell lines was confirmed. For nine of the cell lines these results support the identity established by serological and chromosomal analyses. For the remaining cell lines they provide the first confirmation of species identity. Isozyme profiles of several cell lines from the same species showed unique characteristics that will be useful in monitoring their identity. Two cell lines (IPRI-OL-7 and IPRI-OL-11) considered to be from Orgyia leucostigma appear to contain isozymes of Choristoneura fumiferana. Other supporting evidence and possible causes of this contamination are discussed. These results demonstrate the usefulness of isozyme profiles for the identification and monitoring of cell cultures.

1976 ◽  
Vol 54 (9) ◽  
pp. 1559-1564 ◽  
Author(s):  
J. Krywienczyk ◽  
S. S. Sohi

The identity of four cell lines (Cf124, Md63, Md108, and Md109) was investigated using the technique of double diffusion. The absorbed antiserum of Cf124 cells formed strong precipitin lines with Choristoneura fumiferana antigen, and the absorbed antisera of Md63, Md108, and Md109 cells gave a strong reaction with the Malacosoma disstria antigen, thus substantiating their species identity. Although the M. disstria cell lines did not show any tissue specificity, they differed from each other in at least one antigen. The antigens from whole larvae of C. fumiferana and M. disstria were more suitable than their hemolymph for serological reactions with the antisera of tissue cultures by double diffusion.


2014 ◽  
Vol 30 (3) ◽  
pp. 377-390 ◽  
Author(s):  
S.S.A. Egena ◽  
R.O. Alao

Biochemical diversity or polymorphism is the occurrence of varieties attributed to biochemical differences which are under genetic control. It has created a leeway for the genetic improvement of farm animals. This is because it can be used as a useful tool for the characterization of livestock breeds and population. This way, the degree of similarity or differences within and between breeds can be ascertained and this differences or similarity are important raw materials for genetic improvement of animals. Data obtained on gene frequencies and genotypes through polymorphism study makes it not only possible to compare the gene stocks of animals, the possible effects of the genes on reproductive and performance traits, but also study genetic variability under different environmental conditions of selection. This study was carried out to review haemoglobin (Hb) polymorphism in selected farm animals with the view of finding out the type of polymorphism observed by starch gel electrophoresis due to variation in the amino acid sequence in the polypeptide chains of Hb. The review showed clearly that there is a gene-controlled diversity in the different farm animals considered. This could serve as a reference point for future studies earmarked for the improvement of the animals possibly via marker-assisted selection.


1986 ◽  
Vol 32 (6) ◽  
pp. 481-486 ◽  
Author(s):  
C. Osothsilp ◽  
R. E. Subden

To obtain NAD-dependent malic enzyme mutants of Schizosaccharomyces pombe, a colony color indicator screening system was developed. Mutants defective for malic acid utilization (mau mutants) are yellow, while wild-type colonies are blue on the defined bromcresol green based indicator medium. NAD-dependent malic enzyme mutants were distinguished from other mau mutants by subsequent, starch gel electrophoresis, spectrophotometry, complementation tests, and intermediate pool analysis with cell-free extracts.


OENO One ◽  
1998 ◽  
Vol 32 (1) ◽  
pp. 17
Author(s):  
Ferjani Ben Abdallah ◽  
Farhat Chibani ◽  
Asma Fnayou ◽  
Abdelwahed Ghorbel ◽  
Jean-Michel Boursiquot

<p style="text-align: justify;">61 tunisian autochton grapevine varieties have been collected for biochemical identification. Isozymes analysis with starch gel electrophoresis technique was used to confirn or to cancel random denominations awarded to the majority of these local varieties. In our conditions, concentrated plant extracts were obtained from vigorous donnant canes newly cut off from selected mother plants during automn. These allowed us to dispose of rigorously interpretable isozyme banding patterns of GPI and PGM systems and to overcome difficulties often related to the use of PGM system. The study of GPII and PGM enzyme systems allowed us to classify the autochton accessions into 16 different groups from which 5 groups containing only 2 or 3 varieties.</p><p style="text-align: justify;">On the other hand, the study of AAT and peroxydase enzyme systems has shown stable and legible isozyme banding patterns allowing to discriminate between equivalent accessions such as Sakasly and Kahli (two black local vines very similar), 3 varieties of Bidh Hamem (Bidh Hamem, Bidh Hamem Rafraf and Bidh Hamem Sfax), and 2 varieties of Bezzoul Kelba Bidha (Sfax and Gabes). In addition, certain varieties having for longtime the same denominations were characterized. A case of point the 4 varieties Khalt meaning mixture (Bouchemma, Abiedh, Mdaouer and Souche 1) and the 3 varieties of Arich (Ahmar, Dressée, and Jerba) were proved to be completely different from each other. In the same way, Bezzoul Khadem has been differed from Hemri variety. The complementary use of berry colour allowed to discriminate between Saouadi, Khdhiri and Jebbi varieties and to subdivise the remainig groups into sub-groups.</p><p style="text-align: justify;">The study of GPI, PGM, AAT and peroxydase isozyme banding patterns in combination with berry colour has led to establish a classification of the 61 autochton varieties into 37 groups including 26 varieties definitely differentiated through the results of this biochemical study.</p>


1964 ◽  
Vol 96 (1-2) ◽  
pp. 110-110
Author(s):  
B. G. Loughton ◽  
P. Rueffel ◽  
H. Stich ◽  
A. S. West

It has been suggested that information on the phylogenetic relationships of genera and species could be obtained by comparing the amino acid sequence in the homologous proteins of different species. This procedure is extremely difficult and time-consuming.However, a relatively rapid characterization of proteins can be obtained by analysing their mobilities with starch-gel electrophoresis and examination of antigenic diversity by the agar gel diffusion technique of Ouchterlony.


1993 ◽  
Vol 3 (4) ◽  
pp. 430-433
Author(s):  
C.E. Greer ◽  
R.E. Schutzki ◽  
A. Fernandez ◽  
J.F. Hancock

Starch gel electrophoresis was used to fingerprint 55 Taxus plants, listed as 21 species and/or cultivars. Plants were analyzed for six enzymes, representing eight putative loci. Within many of the cultivars, different fingerprints were observed, indicating nomenclatural errors in Taxus.


1974 ◽  
Vol 52 (11) ◽  
pp. 1073-1078 ◽  
Author(s):  
D. J. Ecobichon

Various techniques, including electrophoresis, gel filtration, titrimetric, and spectrophotometric analysis with specific and nonspecific substrates and inhibitors, were used to characterize the serum esterases of male and female cats. Starch-gel electrophoresis yielded five bands of activity: three butyrylcholinesterase bands and two bands of nonspecific carboxylesterase activity. Gel filtration on Sephadex G-200 yielded two distinct peaks of activity, one containing the cholinesterase bands and the other, the carboxylesterase activity. Kinetic characteristics determined for feline serum esterases included: (1) optimal pH; (2) optimal substrates for cholinesterase and carboxylesterase activities; (3) Km values for the choline, α-naphthyl, and p-nitrophenyl esters. With the organophosphate paraoxon as a specific substrate for arylesterase activity, low levels of this enzyme could be detected in close association with the carboxylesterase.


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