Studies on the relation between plasma antithrombin and heparin-cofactor

1968 ◽  
Vol 46 (3) ◽  
pp. 347-350 ◽  
Author(s):  
F. C. Monkhouse ◽  
Susan Milojevic
Keyword(s):  
Gel Electrophoresis ◽  
Specific Activity ◽  
Deae Cellulose ◽  
Fold Increase ◽  
Significant Loss ◽  
Starch Gel Electrophoresis ◽  
Electrophoretic Patterns ◽  
Starch Gel ◽  
Cofactor Activity ◽  
Cellulose Column

A method for the preparation of purified plasma antithrombin and heparin-cofactor is described. The method involves adsorption by aluminium hydroxide, separation on a DEAE-cellulose column by means of a graded salt concentration, and vertical curtain electrophoresis. A 100-fold increase in the specific activity of antithrombin and a 30-fold increase in the specific activity of heparin-cofactor have been achieved. In spite of the increased purification, no separation of the two activities was achieved. When a highly purified fraction was subjected to starch-gel electrophoresis for 16–18 h and then eluted from the gel, there was significant loss of heparin-cofactor activity but not of antithrombin activity. The electrophoretic patterns of the recovered proteins were not altered.

scholarly journals A chromatographic preparation of ox growth hormone

1966 ◽  
Vol 100 (3) ◽  
pp. 593-600 ◽  
Author(s):  
M Wallis ◽  
HBF Dixon
Keyword(s):  
Molecular Weight ◽  
Growth Hormone ◽  
Gel Electrophoresis ◽  
Anterior Pituitary ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Starch Gel Electrophoresis ◽  
Highly Active ◽  
Cross Linkage ◽  
Starch Gel

1. A method is described for the chromatographic preparation of ox growth hormone. It involves chromatography of an extract of anterior pituitary lobes on DEAE-cellulose, followed by rechromatography on a dextran gel of low cross-linkage (Sephadex G-100). 2. The product is highly active in growth-hormone assays, and is obtained in good yield. It was homogeneous by several criteria, but showed some heterogeneity on starch-gel electrophoresis. 3. The molecular weight of the hormone was estimated from its behaviour on gel-filtration columns under various conditions. Evidence that the hormone may dissociate into sub-units under some conditions is presented.

scholarly journals Erythrocyte glutathione S-transferase. Electrophoretic identification of two enzyme forms

1983 ◽  
Vol 215 (1) ◽  
pp. 213-216 ◽  
Author(s):  
R C Strange ◽  
P H Hirrell ◽  
G A Kitley ◽  
D A Hopkinson ◽  
W Cotton
Keyword(s):  
Enzyme Activity ◽  
Individual Differences ◽  
Gel Electrophoresis ◽  
Human Erythrocytes ◽  
Starch Gel Electrophoresis ◽  
Glutathione S Transferase ◽  
Electrophoretic Patterns ◽  
Starch Gel

Starch-gel electrophoresis was used to demonstrate two forms of glutathione S-transferase in human erythrocytes. Whereas considerable inter-individual differences in enzyme activity and electrophoretic patterns were detected, intra-individual differences were small.

STUDIES ON PLASMINOGEN: IV. ALTERATION OF BOVINE AND HUMAN PLASMINOGENS DURING ISOLATION

1966 ◽  
Vol 44 (4) ◽  
pp. 469-473 ◽  
Author(s):  
John Y. S. Chan ◽  
Edwin T. Mertz
Keyword(s):  
Ionic Strength ◽  
Gel Electrophoresis ◽  
Deae Cellulose ◽  
Starch Gel Electrophoresis ◽  
Major Band ◽  
Starch Gel ◽  
Human Plasminogen

Bovine and human plasminogen preparations were analyzed by starch-gel electrophoresis at pH 2.5 and 0.10 ionic strength. The bands were activated with urokinase and the proteolytic and esterolytic activities measured. Bovine euglobulin contains one plasminogen band, B-1. Plasminogen prepared from bovine euglobulin by continuous electrophoresis at pH 3.5 contains B-1 and a faster plasminogen band, B-2. B-1 and B-2 are also found in bovine plasminogen prepared by DEAE-cellulose chromatography. All three preparations on activation give the same two plasmin bands on starch gel. Human euglobulin also contains two active plasminogen bands H-1 and H-2. Plasminogen prepared from human euglobulin by continuous electrophoresis at pH 3.5 contains H-1, H-2, and a faster minor plasminogen band, H-3. All highly purified human plasminogens derived from Cohn fraction III contain either H-3 as a major band and an additional plasminogen band, H-4, or only H-3, but no H-1 and H-2. On activation with urokinase or streptokinase, human plasminogen preparations give one or two plasmin bands. It is concluded that bovine B-2 and human H-3 and H-4 are altered forms of euglobulin plasminogen created during isolation procedures. Essentially pure human H-3 can be prepared by continuous electrophoresis from Cutter plasminogen.

Benzylamine oxidase and histaminase: purification and crystallization of an enzyme from pig plasma

1964 ◽  
Vol 161 (983) ◽  
pp. 153-167 ◽  
Keyword(s):  
Ammonium Sulphate ◽  
Gel Electrophoresis ◽  
Copper Content ◽  
Deae Cellulose ◽  
Starch Gel Electrophoresis ◽  
Anaerobic Conditions ◽  
Concentrated Solutions ◽  
Radioactivation Analysis ◽  
Starch Gel ◽  
Benzylamine Oxidase

The enzyme benzylamine oxidase of pig plasma has been purified and some of the properties of the pure preparation have been studied. The purification procedure included several precipitations with ammonium sulphate and separations of proteins by column chromatography, first on DEAE-cellulose, followed by DEAE-Sephadex and lastly on a hydroxyapatite column. Crystals were prepared from solutions of the purified enzyme by adding ammonium sulphate. The crystalline preparation was homogeneous when studied by starch-gel electrophoresis and by ultracentrifugation. The molecular weight, as determined on the analytical ultracentrifuge, was 195 000. The copper content of the enzyme, as determined by radioactivation analysis, was about four atoms of Cu per molecule of enzyme. Concentrated solutions of the enzyme had a pink colour; the colour disappeared when substrate (benzylamine) was added under anaerobic conditions. The amines which were tested and found to be oxidized by the pure enzyme were: benzylamine, histamine, mescaline and 4-picolylamine. The affinity of the enzyme for benzylamine was more than one hundred times that for histamine.

scholarly journals Genetic variation in the triploids of Japanese Fasciola species, and relationships with other species in the genus

1994 ◽  
Vol 68 (3) ◽  
pp. 181-186 ◽  
Author(s):  
T. Agatsuma ◽  
K. Terasaki ◽  
L. Yang ◽  
D. Blair
Keyword(s):  
United States Of America ◽  
Gel Electrophoresis ◽  
Laboratory Strain ◽  
Morphological Type ◽  
The United States ◽  
Starch Gel Electrophoresis ◽  
Isozyme Patterns ◽  
Electrophoretic Patterns ◽  
Starch Gel ◽  
Liver Flukes

AbstractTwelve enzymes (encoded by 14 loci) in liver flukes of Fasciola species originating from Japan (parthenogenetic triploids), Korea (parthenogenetic diploids), the United States of America (USA) and Australia (all sexual diploids) were analysed using starch gel electrophoresis. Variation in electrophoretic patterns between samples was detected at five enzyme loci (Ak, Got, Gpi, 6-Pgd and Pgm-2). Japanese worms (31, of which six were established as uniparental laboratory strains), which reproduce by parthenogenesis, exhibited three different isozyme patterns. This indicates that triploidy has arisen more than once in Japanese flukes. Japanese Fasciola sp. can be separated into three types on morphological grounds. For the six laboratory strains of Japanese worms, the parental morphological type was known. Each of the three isozyme patterns observed was restricted to one morphological type. Most alleles detected in the Japanese triploids were also found in diploid worms from the other countries: the only alleles not represented elsewhere were four at the Got locus and two at the Pgm locus. Flukes from a laboratory strain derived from a single Korean diploid worm resembled the Japanese worms in genotype more closely than did American (seven uniparental laboratory strains) or Australian (30 worms) specimens. Worms from the last two countries were closely related.

CHARACTERISTIC ELECTROPHORETIC PATTERNS OF SERUM PROTEINS OF SEVERAL SPECIES OF SNAKES OF IRAN

1965 ◽  
Vol 43 (4) ◽  
pp. 459-461 ◽  
Author(s):  
M. Latifi ◽  
K. D. Shamloo ◽  
A. Amin
Keyword(s):  
Gel Electrophoresis ◽  
Serum Proteins ◽  
Starch Gel Electrophoresis ◽  
Gel Method ◽  
Electrophoretic Patterns ◽  
Starch Gel

Paper and starch-gel electrophoresis of serum proteins of several species and subspecies of poisonous and nonpoisonous snakes of Iran have been investigated. The patterns obtained, especially by means of the starch-gel method, are characteristic for each species. Electrophoretic patterns of samples of serum from different individuals of the same species were very similar.

A COMPARISON OF HISTONES FROM CHICKEN TISSUES BY ZONE ELECTROPHORESIS IN STARCH GEL

1961 ◽  
Vol 39 (3) ◽  
pp. 485-491 ◽  
Author(s):  
J. M. Neelin ◽  
G. C. Butler
Keyword(s):  
Cell Differentiation ◽  
Ionic Strength ◽  
Gel Electrophoresis ◽  
The Other ◽  
Starch Gel Electrophoresis ◽  
Electrophoretic Patterns ◽  
Zone Electrophoresis ◽  
Starch Gel ◽  
Chicken Erythrocytes ◽  
Characteristic Zone

Histories were extracted at pH 1.7 from washed nuclei of chicken erythrocytes, spleen, liver, and testis and compared by starch-gel electrophoresis at pH 5.0, ionic strength 0.020. Spleen and liver histories displayed the most complex electrophoretic patterns with 18 zones each and differed only in relative proportions of certain zones. Erythrocyte histone contained a characteristic zone while lacking a group present in spleen and liver histones. Testis histone with only seven zones differed markedly from the other three. These results were consistent with chromatograms of erythrocyte, spleen, and liver histones on sodium IRC-50. The suggested correlation of tissue-specific histones with cell differentiation is discussed.

Ontogenetic Variation in the Multiple Hemoglobins of Coho Salmon (Oncorhynchus kisutch) and Effect of Environmental Factors on Their Expression

1976 ◽  
Vol 33 (5) ◽  
pp. 1144-1149 ◽  
Author(s):  
M. A. Giles ◽  
W. E. Vanstone
Keyword(s):  
Environmental Factors ◽  
Dissolved Oxygen ◽  
Gel Electrophoresis ◽  
Coho Salmon ◽  
Oncorhynchus Kisutch ◽  
Yolk Sac ◽  
Ontogenetic Variation ◽  
Starch Gel Electrophoresis ◽  
Electrophoretic Patterns ◽  
Starch Gel

Hemolyzates from the blood of coho salmon (Oncorhynchus kisutch) at various stages of development were subjected to micro-starch-gel electrophoresis. Three distinct electrophoretic patterns composed of different combinations of 18 hemoglobin tetramers were observed. Embryonic and yolk-sac alevins possessed 1 cathodic and 12 anodic components while fry retained only 3 of the 12 anodic polymorphs. During smoltification, 4 new cathodic components appeared and 2 of the anodic and the cathodic components of alevin hemolyzates reappeared. This latter pattern was retained until the fish spawned and died. Attempts to induce changes in the pattern of development of these hemoglobins by exposing fry and pre-smolts to extreme variations in dissolved oxygen, temperature, and salinity were completely unsuccessful.

scholarly journals An Improved Chromatographic Separation of Wheat Gluten Proteins

1965 ◽  
Vol 18 (1) ◽  
pp. 193 ◽  
Author(s):  
CW Wrigley
Keyword(s):  
Column Chromatography ◽  
Chromatographic Separation ◽  
Gel Electrophoresis ◽  
Carboxymethyl Cellulose ◽  
Wheat Gluten ◽  
Starch Gel Electrophoresis ◽  
Gluten Proteins ◽  
Electrophoretic Patterns ◽  
Starch Gel

Gel electrophoresis is at present the best procedure for the analytical fractiona-tion of wheat gluten proteins. Procedures more suitable for preparative studies, such as gel ffitration and column chromatography, have provided only partial fractionation on the basis of gel electrophoresis (Graham 1963; Lee et al. 1963; Wright, Brown, and Bell 1964). Gel electrophoretic patterns of fractions resulting from the carboxymethyl cellulose (CMC) fractionation of Simmonds and Winzor (1961) have been published by Graham (1963) and by Lee et al. (1963). These results showed that each fraction was heterogeneous, with considerable overlapping of electrophoretic bands from neighbouring fractions, and that fractions eluted late in the chromatogram were contaminated because of tailing of earlier fractions. The modification of the Simmonds and Winzor procedure described below results in an improved fractionation of gluten proteins as judged by starch-gel electrophoresis.

scholarly journals The separation and characterization of marmoset kidney β-d-galactosidase and β-d-glucosidase

1977 ◽  
Vol 167 (3) ◽  
pp. 765-773 ◽  
Author(s):  
R J Pierce ◽  
R G Price
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Apparent Molecular Weight ◽  
Exchange Chromatography ◽  
Starch Gel Electrophoresis ◽  
Lysosomal Fraction ◽  
Glucosidase Activity ◽  
Starch Gel

beta-D-Galactosidase and beta-D-glucosidase activities were determined in homogenates of marmoset kidney by using the appropriate 4-methylumbelliferyl glycoside, beta-D-Galactosidase activity was separated into two main components by ion-exchange chromatography on DEAE-cellulose, starch-gel electrophoresis, isoelectric focusing and gel filtration on Sephadex G-200. One form designated A had a pI of 5.1, was loosely bound to DEAE-cellulose at pH7.0, remained near the origin on starch-gel electrophoresis at pH 7.0 and had an apparent molecular weight of 160000. The second beta-D-galactosidase component, designated B, was associated with the total beta-D-glucosidase activity, had a pI of 4.3, was firmly bound to DEAE-cellulose, migrated rapidly towards the anode on starch-gel electrophoresis and had an apparent molecular weight of 50000. The optimum pH values of beta-D-galactosidase A and B were 4.5 and 6.0 respectively. beta-D-Galactosidase A was activated by 0.1 M-NaC1 but the activity of the B form was inhibited by 1 M-NaC1 at pH 4.5. beta-D-galactosidase had a bimodal distribution, the A form being recovered in the lysosomal fraction whereas the B form was present in the soluble fraction, as was the major portion of the beta-D-glucosidase activity. The lysosomal and soluble forms were further characterized by DEAE-cellulose chromatography.

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