Esterases of the flounder (Platichthys flesus, Pleuronectidae, Teleostei): Development of an identification protocol using starch gel electrophoresis and characterization of loci

1990 ◽  
Vol 46 (8) ◽  
pp. 863-867 ◽  
Author(s):  
P. Berrebi ◽  
P. Landaud ◽  
P. Borsa ◽  
J. F. Renno
Keyword(s):  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Platichthys Flesus ◽  
Starch Gel

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.

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.

scholarly journals Characterization of Enterobacteria by Starch-Gel Electrophoresis of Glucose-6-Phosphate Dehydrogenase and Phosphogluconate Dehydrogenase

1967 ◽  
Vol 94 (3) ◽  
pp. 544-551 ◽  
Author(s):  
James E. Bowman ◽  
Robert R. Brubaker ◽  
Henri Frischer ◽  
Paul E. Carson
Keyword(s):  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Phosphogluconate Dehydrogenase ◽  
Starch Gel ◽  
Glucose 6 Phosphate Dehydrogenase

scholarly journals Isolation and Characterization of Protein Bodies From Developing Wheat Endosperm

1963 ◽  
Vol 16 (2) ◽  
pp. 375 ◽  
Author(s):  
Janet SD Graham ◽  
RK Morton ◽  
JK Raison
Keyword(s):  
Electron Microscopy ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Separation And Purification ◽  
Isolation And Characterization ◽  
Dense Bodies ◽  
Starch Gel ◽  
Slow Moving ◽  
Protein Components

Procedures are described for separation and purification of electron-dense bodies previously observed in intact endosperm by electron microscopy. Isolated bodies consist largely of protein. By starch-gel electrophoresis, the bodies contain predominantly slow-moving protein components similf1l' to those found in acetic acid extracts of whole endosperm.

scholarly journals Characterization of tissue alkaline phosphatases and their partial purification by starch-gel electrophoresis

1961 ◽  
Vol 81 (2) ◽  
pp. 441-447 ◽  
Author(s):  
DW MOSS ◽  
DM CAMPBELL ◽  
E ANAGNOSTOU-KAKARAS ◽  
EJ KING
Keyword(s):  
Gel Electrophoresis ◽  
Partial Purification ◽  
Starch Gel Electrophoresis ◽  
Alkaline Phosphatases ◽  
Starch Gel

scholarly journals Starch-gel Electrophoresis in the Characterization of Products of Collagen Breakdown.

1967 ◽  
Vol 21 ◽  
pp. 827-827 ◽  
Author(s):  
R. Penttinen ◽  
A. Kari ◽  
E. Kulonen ◽  
Åke Nilsson ◽  
H. Theorell ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Starch Gel

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 PHYSICOCHEMICAL CHARACTERIZATION OF MOUSE MYELOMA PROTEINS: DEMONSTRATION OF HETEROGENEITY FOR EACH MYELOMA GLOBULIN

1961 ◽  
Vol 114 (3) ◽  
pp. 399-413 ◽  
Author(s):  
John L. Fahey
Keyword(s):  
Gel Electrophoresis ◽  
Physicochemical Characterization ◽  
Physicochemical Characteristics ◽  
Starch Gel Electrophoresis ◽  
Myeloma Protein ◽  
Myeloma Proteins ◽  
Wide Range ◽  
Starch Gel ◽  
Mouse Myeloma

Physicochemical characterization of mouse myeloma proteins revealed the individuality of each myeloma protein. When the myeloma proteins are considered collectively a wide range of individual properties were represented, including electrophoretic mobilities varying from the gamma to alpha region, hexose contents from 1 to 4 per cent, and ultracentrifugal components from 6.5 to 13 S. The 20 myeloma proteins could be divided into groups, the gamma type and the beta type myeloma globulins, on the basis of physicochemical, as well as immunoelectrophoretic, studies. Two gamma type myeloma proteins (5563, MPC-11) resembled normal gamma globulins, sedimenting as a single 6.5 S peak in the ultracentrifuge, and having a relatively low hexose content (1 per cent). Eighteen beta type mouse myeloma proteins differed from gamma myeloma proteins and, typically, were found on ultracentrifugal analysis to have multiple components with sedimentation coefficients of 6.5, 9, 11, and 13 S, having a higher hexose content (2 to 4 per cent) as well as distinctive chromatographic and starch gel electrophoretic properties. All of the mouse myeloma proteins were heterogeneous and heterogeneity of two types was observed. Polymer formation was responsible for the 9, 11, and/or 13 S components seen on ultracentrifugation of the beta type myeloma proteins. Starch gel electrophoresis revealed this type of heterogeneity as relatively widely separated myeloma protein components, presumably owing to the retardation effect of starch gel on the electrophoretic migration of the larger polymers. Starch gel electrophoresis revealed a different type of heterogeneity for the two gamma type myeloma proteins, each of these being shown to contain 5 or more components differing only in electrophoretic properties. The physicochemical characteristics of the γ-type and ß-type myeloma proteins in the mouse indicated the close similarity of these proteins to the γ- and ß-2A-myeloma proteins in man.

Enzymatic Modifications of the Protamines. II. Separation and Characterization of Phosphorylated Species of Protamines from Trout Testis

1974 ◽  
Vol 52 (6) ◽  
pp. 536-546 ◽  
Author(s):  
Andrew J. Louie ◽  
Gordon H. Dixon
Keyword(s):  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Stage Of Development ◽  
Phosphorylated Amino Acid ◽  
Similar Series ◽  
Starch Gel ◽  
Derivatives Of

Substantial quantities of highly phosphorylated protamines were prepared from hormonally induced trout testes at the early protamine stage of development. Purified protamines from testes induced to mature by injection of salmon pituitary extracts were resolved into eight fractions on long carboxymethyl cellulose columns by eluting with a gradient of LiCl in the presence of 6 M urea; only two major fractions were found in protamine extracted from naturally maturing testes. Each fraction was not homogenous but consisted of a mixture of several related protamines. Analysis of radioactivity in in vivo32P-labeled protamine indicated that six of the eight fractions were phosphorylated. Amino acid analysis, phosphate determinations, and starch gel electrophoresis indicated that three of the phosphorylated peaks correspond to the mono-, di-, and triphosphorylated derivatives of the first fraction (three serines) of protamine, while the other three correspond to a similar series of the second fraction (four serines) of protamine. These protamines with differing levels of phosphorylation may be useful for in vitro studies of the interaction of phosphoprotamines with DNA or chromatin.

Characterization of human liver ferritin by starch-gel electrophoresis

1963 ◽  
Vol 8 (1) ◽  
pp. 165-167 ◽  
Author(s):  
J.J. Theron ◽  
A.O. Hawtrey ◽  
V. Schirren
Keyword(s):  
Gel Electrophoresis ◽  
Human Liver ◽  
Starch Gel Electrophoresis ◽  
Human Liver Ferritin ◽  
Starch Gel ◽  
Liver Ferritin
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