The labelling of certain milk proteins with iodine131

1965 ◽  
Vol 32 (2) ◽  
pp. 181-186 ◽  
Author(s):  
H. A. Veringa ◽  
M. F. Kerkhof Mogot
Keyword(s):  
Gel Electrophoresis ◽  
Milk Proteins ◽  
Starch Gel Electrophoresis ◽  
Molecular Weights ◽  
Fat Globules ◽  
Starch Gel ◽  
Clustering Effect ◽  
Β Lactoglobulin ◽  
Electrophoresis Pattern

SummaryWhole casein, β-casein, β-lactoglobulin and euglobulin were labelled with 131I. The conditions under which iodination was carried out were chosen so as to avoid any modification of the original characteristics of the proteins. This was checked by starch-gel electrophoresis and determination of sedimentation constants, apparent molecular weights and, for euglobulin, the clustering effect on fat globules.As was shown by autoradiograms of the starch-gel plates, the radioactivity was incorporated in all zones of the electrophoresis pattern.

scholarly journals Die Trennung der Hämolymphe-Proteine bei Vorpuppen und Puppen der Galleria mellonella L. mittels Gel-Filtration auf Sephadex G-200, Bestimmung ihrer isoelektrischen Punkte und ihrer Molekulargewichte / Separation of Haemolymph Proteins of Prepuae and Pupae of Galleria mellonella L. by means of Gel Filtration on Sephadex 200, Determination of their Isoelectric Points and their Molecular Weights

1969 ◽  
Vol 24 (6) ◽  
pp. 732-740 ◽  
Author(s):  
Milan Marek
Keyword(s):  
Gel Electrophoresis ◽  
Galleria Mellonella ◽  
Gel Filtration ◽  
Starch Gel Electrophoresis ◽  
Molecular Weights ◽  
Isoelectric Points ◽  
Starch Gel ◽  
The Individual ◽  
Naphthyl Acetate

Gel filtration on Sephadex G-200 was carried out on haemolymph proteins of prepupae. ligatured prepupae, male and female pupae and cooled pupae of Galleria mellonella L.The proteins were separated into two main fractions. The esterase activity of the eluated haemolymph was determined by means of beta-naphthyl acetate after filtration.After elution the samples were condensed and additionally separated on horizontal starch-gel electrophoresis.The “cooling protein” of pupae and the “ligature protein” of ligatured larvae of Galleria mellonella were shown by means of starch-gel electrophoresis to be new proteins, so far not described.The isoelectric point and molecular weight were determined for the individual protein fractions.They were then stained with amido black 10 B for the proof of proteins, and with alpha-naphthyl butyrate with Fast-Blue BB salt for the identification of esterases.

Improved Method for the Determination of Hemoglobin A2 by Starch-Gel Electrophoresis

1960 ◽  
Vol 6 (3) ◽  
pp. 254-262 ◽  
Author(s):  
C A J. Goldberg ◽  
A C Ross
Keyword(s):  
Sickle Cell ◽  
Gel Electrophoresis ◽  
Sickle Cell Trait ◽  
Starch Gel Electrophoresis ◽  
Improved Method ◽  
Starch Gel ◽  
Thalassemia Trait ◽  
Healthy Persons ◽  
Hemoglobin A2

Abstract It has been shown that variations in the preparation of the starch gel and in photographic interpretation can significantly affect the accuracy of the measurement of hemoglobin A2. An improved method for the determination of hemoglobin A2 by starch-gel electrophoresis has been presented which affords greater accuracy than was previously achieved. Hemoglobin A2 concentrations for healthy persons and patients with sickle cell trait, various nonthalassemic anemias, and thalassemia trait have been presented.

A New Method for Starch Gel Electrophoresis of Human Hemoglobins, with Special Reference to the Determination of Hemoglobin A2

1958 ◽  
Vol 4 (6) ◽  
pp. 484-495 ◽  
Author(s):  
C A J Goldberg
Keyword(s):  
Special Reference ◽  
Gel Electrophoresis ◽  
New Method ◽  
Resolving Power ◽  
Buffer System ◽  
Starch Gel Electrophoresis ◽  
Healthy Individuals ◽  
Starch Gel ◽  
Hemoglobin A2

Abstract A method for starch gel electrophoresis of hemoglobins is presented in which a modified Lintner starch is used for the preparation of the gel. A discontinuous buffer system of tris-EDTA-borate/barbital is used as the electrolyte medium because of its superior resolving power. Hemoglobin A2 values, obtained with this method, of healthy individuals, patients with thalassemia, and those with various anemias of nonthalassemic origin are presented.

scholarly journals Some relationships between R-factor and chromosomal β-lactamase in Gram-negative bacteria

1971 ◽  
Vol 123 (4) ◽  
pp. 507-512 ◽  
Author(s):  
J. W. Dale ◽  
J. T. Smith
Keyword(s):  
Gel Electrophoresis ◽  
Klebsiella Aerogenes ◽  
Gram Negative Bacteria ◽  
Starch Gel Electrophoresis ◽  
Gram Negative ◽  
E Coli ◽  
Molecular Weights ◽  
R Factor ◽  
Starch Gel ◽  
R Factors

1. The β-lactamases specified by Klebsiella aerogenes 418 and the R-factor R-7268 have been partially purified. 2. The molecular weights of the K. aerogenes strains 418 and 373, Aerobacter cloacae 53, R-7268 and R-TEM β-lactamases were all about 20000; that of the enzymes from Escherichia coli strains 419 and 214T was about 31000. 3. These enzymes were also compared by means of their Km values for benzylpenicillin and ampicillin, and their behaviour on starch-gel electrophoresis. 4. The β-lactamases specified by the two Klebsiella strains, the Aerobacter strain, and the R-factors R-TEM and R-7268 were found to comprise a broadly similar group. However, within this group, only two enzymes seemed to be identical, namely those specified by the two R-factors. The two E. coli strains produce identical β-lactamases which are very different from the ‘Klebsiella/Aerobacter-type’ enzymes.

scholarly journals The determination of lactate dehydrogenase isoenzymes in normal human muscle and other tissues

1967 ◽  
Vol 105 (2) ◽  
pp. 599-604 ◽  
Author(s):  
A. E. H. Emery
Keyword(s):  
Lactate Dehydrogenase ◽  
Gel Electrophoresis ◽  
Human Muscle ◽  
Starch Gel Electrophoresis ◽  
Fibrous Connective Tissue ◽  
Starch Gel ◽  
Normal Human ◽  
Lactate Dehydrogenase Isoenzymes ◽  
Good Agreement

1. A technique has been developed, based on preferential inhibition by urea, for determining the amounts and proportions of the M and H sub-units of lactate dehydrogenase (referred to as LDH-M and LDH-H respectively) in human tissues, including muscle. 2. There was good agreement between the results obtained with urea inhibition and those obtained with starch-gel electrophoresis. 3. With increasing age there was a significant decrease in the total amount of lactate dehydrogenase and the amount of LDH-M in skeletal muscle. This could not be accounted for by the replacement of functioning muscle tissue by fibrous connective tissue. 4. The proportion of LDH-M was less in certain muscles (e.g. soleus and extra-ocular) than in other muscles (e.g. gastrocnemius and rectus abdominis). 5. The proportions of LDH-M and LDH-H did not differ significantly in different superficial limb muscles and were not significantly affected by either age or sex. 6. Specimens of muscle from 86 different individuals (all Europeans) have been subjected to electrophoresis, but no variants of lactate dehydrogenase isoenzymes have been found.

STUDIES ON PLASMINOGEN: VI. ACTIVATION PRODUCTS OF BOVINE AND HUMAN PLASMINOGENS

1966 ◽  
Vol 44 (4) ◽  
pp. 487-495 ◽  
Author(s):  
John Y. S. Chan ◽  
Edwin T. Mertz
Keyword(s):  
Gel Electrophoresis ◽  
Elution Curve ◽  
Major Protein ◽  
Starch Gel Electrophoresis ◽  
Sephadex Column ◽  
Molecular Weights ◽  
Activation Products ◽  
Starch Gel ◽  
Human Plasminogen

Activated, purified bovine plasminogen, when fractionated on a Sephadex column, revealed four major protein peaks. Bovine plasmin I and plasmin II were found under peak II and peak III, respectively. Highly potent bovine plasmin II was recovered from peak III. Activated human plasminogen, when fractionated by the same technique, yielded an elution curve similar to that of the nonactivated sample. The pathway of the breakdown of bovine plasminogen upon activation with urokinase was studied by starch-gel electrophoresis and Sephadex chromatography. It is suggested that native bovine plasminogen is first converted to an altered plasminogen, which is then converted to plasmin I, plasmin I is then converted to plasmin II, and plasmin II to peptide A. The molecular weights of plasmin I, plasmin II, and peptide A were estimated by the Sephadex method to be 8.0 × 104, 6.2 × 104, and 4.3 × 104, respectively.

A QUANTITATIVE METHOD FOR THE DETERMINATION OF CHOLINESTERASE ACTIVITY AFTER STARCH-GEL ELECTROPHORESIS

1966 ◽  
Vol 44 (6) ◽  
pp. 953-955 ◽  
Author(s):  
H. S. Funnell ◽  
W. T. Oliver
Keyword(s):  
Gel Electrophoresis ◽  
Quantitative Method ◽  
Cholinesterase Activity ◽  
Competitive Inhibition ◽  
Starch Gel Electrophoresis ◽  
Final Solution ◽  
Natural Activity ◽  
Starch Gel ◽  
Hydrolysis Of

The method described in this paper is based upon hydrolysis of the starch gel by sodium hydroxide, which releases the dye. The dye is then taken up in an immiscible solvent, and the color determined spectrophotometrically. The method gave good reproducibility in studies both of natural activity and competitive inhibition without requiring any changes in the usual methods. The amount of dye in the final solution was related to the activity towards the dye-producing substrate of the enzyme present in the gel section.

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