CHARACTERIZATION OF THE ESTERASES FROM ELECTRIC TISSUE OF ELECTROPHORUS BY STARCH-GEL ELECTROPHORESIS

1967 ◽  
Vol 45 (7) ◽  
pp. 1099-1105 ◽  
Author(s):  
D. J. Ecobichon ◽  
Y. Israel
Keyword(s):  
Electrophoretic Mobility ◽  
Gel Electrophoresis ◽  
Water Soluble ◽  
Starch Gel Electrophoresis ◽  
Electrophorus Electricus ◽  
Vertical Zone ◽  
Zone Electrophoresis ◽  
Starch Gel

The water-soluble esterases of a microsome-free supernatant of the electric tissue of Electrophorus electricus were separated by vertical-zone electrophoresis in starch gel. Specific and nonspecific substrates and inhibitors were used in conjunction with histochemical techniques to identify the enzymes. Acetylcholinesterase was present in the form of four bands of activity, the electrophoretic mobility of which was suggestive of aggregated forms of the enzyme. Pseudocholinesterase was detected as two weak bands of activity. A third esterase was identified as a nonspecific carboxylesterase and shown to be a sialoprotein.

scholarly journals ENZYMATICALLY PRODUCED SUBUNITS OF PROTEINS FORMED BY PLASMA CELLS IN MICE

1962 ◽  
Vol 115 (3) ◽  
pp. 623-639 ◽  
Author(s):  
J. L. Fahey ◽  
Brigitte A. Askonas
Keyword(s):  
Electrophoretic Mobility ◽  
Gel Electrophoresis ◽  
Gamma Globulin ◽  
Immunological Methods ◽  
Antigenic Determinants ◽  
Antibody Activity ◽  
Starch Gel Electrophoresis ◽  
Myeloma Protein ◽  
Γ Globulins ◽  
Starch Gel

Gamma globulin and antibody obtained from inbred C3H mice are split by papain and cysteine into fragments roughly one-third the size of the original Molecule (S20,w = 3.5S). The papain digests were characterized by starch gel electrophoresis and immunological methods. The highly heterogeneous fragments could be divided into two groups with distinct antigenic determinants (S and F), which were separated by DEAE ion-exchange cellulose chromatography. Approximately two-thirds of the fragments had S antigenic groupings and one-third had F antigenic groupings. These data are consistent with the view that mouse gamma globulin is split by papain and cysteine into three major fragments, two of which are of the S type and one of the F type. Antibody activity of the original molecule was present in the S fragments. Although the S fragments did not precipitate the antigen (hemocyanin) they were shown to bind antigen specifically in the manner of univalent antibodies. The S fragments of normal γ-globulin were very heterogeneous with a broad spectrum of electrophoretic mobilities. Comparison of S fragments from slow and fast migrating globulins showed that the mobilities of the original γ-globulin samples were largely reflected in the mobilities of their S fragments. Additional observations indicated that the F fragments also may help to determine the electrophoretic mobility of intact γ-globulin molecules. S fragments of differing electrophoretic mobility were shown to have the same antigenic determinants, indicating that the structural differences responsible for the electrophoretic mobility differences were not involved in the antigenic groupings identified with rabbit antisera. The F fragments of normal γ-globulin migrated more rapidly than the S fragments, were less heterogeneous, and showed several bands on starch gel electrophoresis. The F fragments differed antigenically from the S fragments, and had no antibody activity. Two groups of F fragments (F and F') were detected with some antisera. The γ-myeloma protein (5563) formed in a C3H plasma cell tumor and similarly fragmented by treatment with papain and cysteine, produced much more discrete S and F components than were found in the normal γ-globulin digest. The electrophoretic properties of the myeloma protein fragments were within the range observed for normal γ-globulin fragments. Although the γ-myeloma protein shares antigenic determinants with normal γ-globulins it lacks some of the antigenic groupings present in the γ-globulin preparation. Both S and F fragments from the myeloma protein share antigenic determinants with the corresponding fragments from normal γ-globulin. In addition, both S and F fragments of normal γ-globulin possess antigenic groupings not present in fragments of the γ-myeloma protein, accounting for the antigenic deficiency observed on comparison of the γ-myeloma protein with normal γ-globulins.

Identification of Australian barley cultivars by laboratory methods: gel electrophoresis and gel isoelectric focusing of the endosperm proteins

1977 ◽  
Vol 17 (89) ◽  
pp. 1020 ◽  
Author(s):  
J McCausland ◽  
CW Wrigley
Keyword(s):  
Isoelectric Focusing ◽  
Gel Electrophoresis ◽  
Water Soluble ◽  
The Other ◽  
Starch Gel Electrophoresis ◽  
Laboratory Methods ◽  
Barley Cultivars ◽  
Starch Gel ◽  
Electrophoretic Techniques ◽  
Gel Isoelectric Focusing

A range of laboratory methods was examined for their ability to distinguish between 19 barley cultivars currently grown in Australia. Aleurone colour, revealed after mechanical or chemical dehulling, differentiated Abyssinian, Atlas, Cape and Corvette from the other cultivars. Peroxidase and phenol testing were not useful. Seven different patterns were obtained for the hordeins of lowest mobility by starch gel electrophoresis. Further distinction was provided by flat gel isoelectric focusing of the water-soluble and hordein proteins for which 13 different pattern-groupings were obtained. The two electrophoretic techniques complemented one another, so that the use of both methods left only a few cultivars that could not be distinguished.

PROPERTIES AND CLASSIFICATION OF THE SOLUBLE ESTERASES OF HUMAN BRAIN

1966 ◽  
Vol 44 (2) ◽  
pp. 225-232 ◽  
Author(s):  
D. J. Ecobichon
Keyword(s):  
Alkaline Phosphatase ◽  
Human Brain ◽  
Esterase Activity ◽  
Water Soluble ◽  
Human Tissues ◽  
Esterase Pattern ◽  
Vertical Zone ◽  
Zone Electrophoresis ◽  
Starch Gel

Water-soluble proteins and enzymes of human brain were separated by vertical zone electrophoresis in starch gel. Fifteen bands of esterase activity were detected in brain. Various substrates and inhibitors were used in efforts to identify enzymes in addition to a comparison of the esterase pattern with patterns obtained from other human tissues. One zone, composed of four bands of acetylesterase activity, was found to be common to all the tissues investigated with the exception of serum. Two bands of cholinesterase and two bands of A-esterase activity were identified. The remaining bands, which were aliesterases possessing broad overlapping substrate specificity and inhibitor sensitivity, were electrophoretically different from those of other tissues. Observations on alkaline phosphatase, acid phosphatase, and lactate dehydrogenase were recorded for comparison with the data on esterases.

Comparative zone electrophoresis of catalase of Staphylococcus species isolated from mammalian skin

1976 ◽  
Vol 22 (12) ◽  
pp. 1691-1698 ◽  
Author(s):  
Raymond J. Zimmerman
Keyword(s):  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Polyacrylamide Electrophoresis ◽  
Electrophoretic Mobilities ◽  
Mammalian Skin ◽  
Zone Electrophoresis ◽  
Starch Gel ◽  
Molecular Sieving

Vertical polyacrylamide slab gel electrophoresis was conducted for the catalase enzymes of representative strains of 18 proposed species and subspecies of the genus Staphylococcus. The catalase bands which resulted were predominantly monomorphic within each of the species and differences in catalase mobilities were observed between many of the species. The electrophoretic mobilities of the catalases were supportive to the scheme of classification used. Many strains of certain species demonstrated multiple catalase bands which are suggestive of multimolecular forms of the enzyme. Horizontal starch gel electrophoresis of representative strains of S. capitis produced catalase bands with relative mobilities that were different from those obtained with polyacrylamide electrophoresis, presumably due to a difference in molecular sieving between the gels.

The Separation of Insect Haemolymph Proteins

1964 ◽  
Vol 96 (1-2) ◽  
pp. 110-110
Author(s):  
B. G. Loughton ◽  
P. Rueffel ◽  
H. Stich ◽  
A. S. West
Keyword(s):  
Amino Acid ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Homologous Proteins ◽  
Agar Gel ◽  
Diffusion Technique ◽  
Starch Gel ◽  
Rapid Characterization ◽  
Gel Diffusion

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.

INFLUENCE OF ALIEN GENOME COMBINATIONS ON PROTEIN SYNTHESIS IN CEREALS

1964 ◽  
Vol 42 (12) ◽  
pp. 1647-1657 ◽  
Author(s):  
F. C. Yong ◽  
A. M. Unrau
Keyword(s):  
Protein Synthesis ◽  
Gel Electrophoresis ◽  
Triticum Durum ◽  
Tetraploid Wheat ◽  
Water Soluble ◽  
Starch Gel Electrophoresis ◽  
Triticum Vulgare ◽  
Qualitative And Quantitative ◽  
Starch Gel ◽  
Variable Influence

Starch-gel electrophoresis of the water-soluble, salt-soluble, and alcohol soluble proteins of Triticale, Triticum durum, Secale cereale, Triticum vulgare, and Tritipyron revealed both qualitative and quantitative differences. The experimental evidence obtained indicated that the biosynthetic potential of the alien genomes in the synthetic species (Triticale) was not fully maintained. A variable influence of the tetraploid wheat (T. durum) genomes on protein synthesis in the three hexaploid cereals (Triticale, T. vulgare, and Tritipyron) was observed.

scholarly journals Electrophoretic Characterization of Taxus Cultivars

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

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.

ZONE ELECTROPHORESIS OF CALF THYMUS HISTONE IN STARCH GEL

1960 ◽  
Vol 38 (4) ◽  
pp. 355-363 ◽  
Author(s):  
J. M. Neelin ◽  
E. M. Neelin
Keyword(s):  
Amino Acids ◽  
Gel Electrophoresis ◽  
Low Ph ◽  
Acid Extraction ◽  
Starch Gel Electrophoresis ◽  
Calf Thymus ◽  
Zone Electrophoresis ◽  
Starch Gel ◽  
Terminal Amino

A total of 19 zones were detected by starch gel electrophoresis of calf thymus histone in buffers of 0.02 μ below pH 5.0. Of these, 18 were evident at pH 4.9 (acetate) and 15 at pH 3.9 (formate). Above pH 5.0, aggregation interfered with resolution, but by adding 4 M urea to the gel sufficient resolution was obtained between pH 4.4 and 8.7 to distinguish a total of 22 zones. Of this total, three fast components were present only occasionally in trace amounts, and three others were resolved from the immobile aggregated histone at low pH only. At least 16 zones appeared to be native histone components. Acid extraction of the histone did not appear to cause degradation since no new N-terminal amino acids were generated by this step. Two different methods of preparation produced histone extracts with essentially the same electrophoretic properties.

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