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

A three step purification procedure for human liver ferritin

1980 ◽  
Vol 58 (6) ◽  
pp. 494-498 ◽  
Author(s):  
M. Pagé ◽  
J. Lagueux ◽  
C. Gauthier
Keyword(s):  
Affinity Chromatography ◽  
Gel Electrophoresis ◽  
Human Liver ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Purification Procedure ◽  
Human Liver Ferritin ◽  
Normal Human Liver ◽  
Normal Human ◽  
Liver Ferritin

We describe a method for the purification of normal human liver ferritin by ultrafiltration, gel filtration on Sephacryl S-300, and affinity chromatography on DEAE-Affi Gel Blue. The purity of the ferritin obtained was verified by immunoelectrophoresis, Ouchterlony immunodiffusion, polyacrylamide gel electrophoresis, and electrofocusing. This rapid method yields 32% of the original ferritin.

scholarly journals Organic pyrophosphates as substrates for human alkaline phosphatases

1967 ◽  
Vol 105 (3) ◽  
pp. 1307-1312 ◽  
Author(s):  
R. Helen Eaton ◽  
D W Moss
Keyword(s):  
Gel Electrophoresis ◽  
Human Liver ◽  
Inorganic Phosphate ◽  
Starch Gel Electrophoresis ◽  
Alkaline Phosphatases ◽  
Starch Gel ◽  
Pyrophosphatase Activity ◽  
Small Intestinal ◽  
Hydrolysis Of ◽  
Single Enzyme

1. Purified human liver and small-intestinal alkaline orthophosphatases release inorganic phosphate at appreciable rates from a variety of organic pyrophosphate substrates. 2. The pyrophosphatase action is inhibited by Mg2+ ions at concentrations that activate the hydrolysis of orthophosphate substrates by these enzymes. 3. The results of mixed-substrate experiments, denaturation studies with heat or urea and starch-gel electrophoresis suggest that both orthophosphatase and pyrophosphatase activities are, in each preparation, properties of a single enzyme. 4. Intestinal phosphatase shows greater pyrophosphatase activity relative to orthophosphatase than the liver enzyme.

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 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 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.

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