Polyacrylamide gel isoelectric focusing of proteins: Determination of isoelectric points using an antimony electrode

1972 ◽  
Vol 285 (2) ◽  
pp. 293-300 ◽  
Author(s):  
J.A. Beeley ◽  
S.M. Stevenson ◽  
J.G. Beeley
Keyword(s):  
Isoelectric Focusing ◽  
Polyacrylamide Gel ◽  
Antimony Electrode ◽  
Isoelectric Points ◽  
Gel Isoelectric Focusing

Isoelectric focusing of insulin, 125I-insulin and the 125I-insulin-antibody complex

1979 ◽  
Vol 44 (6) ◽  
pp. 1828-1834
Author(s):  
Asja Šiševa ◽  
Jiřina Slaninová ◽  
Tomislav Barth ◽  
Stephan P. Ditzov ◽  
Luben M. Sirakov
Keyword(s):  
Isoelectric Focusing ◽  
Polyacrylamide Gel ◽  
The Other ◽  
Insulin Antibody ◽  
Isoelectric Points ◽  
Antibody Complex ◽  
And Storage ◽  
Acid Region ◽  
Three Components

Isoelectric focusing on polyacrylamide gel columns of three native crystalline commercial preparations of insulin and 125I-labelled insulin was carried out. All the compounds studied contained three components of different isoelectric points. The largest fraction, having pI 5.60 ± 0.05, was common to all preparations. The other two fractions were situated in the acid region of pH between pI 4.5 and 5.2. The presence of these fractions is explained by the contamination of crystalline insulins by proinsulin and by the formation of des-amido derivatives during the dissolving and storage of insulin samples, and, in case of labelled insulin, also by the presence of heavily iodinated insulin and contaminating components. The isoelectric focusing of the complex 125I-insulin-antibody showed a peak of radioactivity having pI 6.15 ± 0.05.

Relation of age to isoenzyme pattern and total activity of amylase in serum.

1981 ◽  
Vol 27 (3) ◽  
pp. 451-454 ◽  
Author(s):  
P J Bossuyt ◽  
R Van den Bogaert ◽  
S L Scharpé ◽  
Y Van Maercke
Keyword(s):  
Thin Layer ◽  
Isoelectric Focusing ◽  
Serum Amylase ◽  
Amylase Activity ◽  
Total Activity ◽  
Ph Gradient ◽  
Isoenzyme Pattern ◽  
Isoelectric Points ◽  
Age Dependent ◽  
Gel Isoelectric Focusing

Abstract Pancreatic and salivary isoenzymes of amylase were determined in serum from 70 subjects. Thin-layer gel/isoelectric focusing was used to separate the isoenzymes. Because other studies (J. Lab. Clin. Med. 90: 141-151, 1977) show that the major isoamylases have isoelectric points between 5.8 and 7.2, we focused the sera on polyacrylamide gel plates with a pH gradient from 5.5 to 8.5. The separated amylase fractions were made visible by direct incubation with a commercially available dye-starch polymer. Isoelectric focusing proved to be convenient, precise, and reproducible, and it can be used as a routine analysis to detect even slight changes in serum amylase distributions. We found that the isoamylase distribution is age dependent, whereas total amylase activity shows no correlation with age.

Detection of the Genetic Polymorphism of Human C2 (Native Protein and C2a Fragment) by Immunoblotting after Polyacrylamide Gel Isoelectric Focusing

Complement ◽  
1985 ◽  
Vol 2 (4) ◽  
pp. 185-192 ◽  
Author(s):  
B. Uring-Lambert ◽  
S. Gas ◽  
J. Goetz ◽  
G. Mauff ◽  
S.F. Goldmann ◽  
...  
Keyword(s):  
Genetic Polymorphism ◽  
Isoelectric Focusing ◽  
Polyacrylamide Gel ◽  
Native Protein ◽  
Gel Isoelectric Focusing

Salivary deoxyribounuclease I polymorphism separated by polyacrylamide gel-isoelectric focusing and detected by the dried agarose film overlay method

1993 ◽  
Vol 14 (1) ◽  
pp. 1042-1044 ◽  
Author(s):  
Etsuko Tenjo ◽  
Kazumi Sawazaki ◽  
Toshihiro Yasuda ◽  
Daita Nadano ◽  
Haruo Takeshita ◽  
...  
Keyword(s):  
Isoelectric Focusing ◽  
Polyacrylamide Gel ◽  
Overlay Method ◽  
Gel Isoelectric Focusing

Fish Species Identification by Isoelectric Focusing: Sarcoplasmic Protein Polymorphism in Monkfish (Lophius americanus)

1981 ◽  
Vol 64 (1) ◽  
pp. 32-37
Author(s):  
Ronald C Lundstrom
Keyword(s):  
Species Identification ◽  
Isoelectric Focusing ◽  
Fish Species ◽  
Protein Pattern ◽  
Polyacrylamide Gel ◽  
Protein Patterns ◽  
Fish Species Identification ◽  
Sarcoplasmic Protein ◽  
Gel Isoelectric Focusing ◽  
Agarose Ief

Abstract Monkfish (Lophius americanus) sarcoplasmic protein patterns were found to be polymorphic with respect to separations using isoelectric focusing. Reproducible protein pattern variations were not detected using cellulose acetate or polyacrylamide gel disc electrophoresis. Monkfish sarcoplasmic proteins separated on pH 3.5-9.5 Ampholine PAGplates or on pH 2.5-9.0 agarose IEF gels yielded similar patterns showing 3 distinct, reproducible variations. On close examination, the pH 3.5-9.5 Ampholine PAGplate patterns could be further subdivided into 3 additional variations. A high resolution pH 3.5-5.0 agarose IEF gel was able to resolve a total of 10 different monkfish pattern variations in a sample of 24 individuals. A model was proposed suggesting the existence of 16 distinct variations in the monkfish sarcoplasmic protein pattern, based on the various combinations of 4 protein bands. In identifying samples of monkfish meat, it is necessary to compare the unknown pattern with the possible variant patterns to effect a reliable identification. On recommendation by the Associate Referee, the method for fish species identification based on polyacrylamide gel isoelectric focusing, 18.A01-18.A04, has been adopted official final action with no restrictions as to the species that may be identified.

Isoelectric points and molecular weights of salt-extractable ribosomal proteins

1976 ◽  
Vol 54 (12) ◽  
pp. 1029-1033 ◽  
Author(s):  
M Saleem ◽  
Burr Atkinson
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Molecular Weights ◽  
Isoelectric Points ◽  
Acidic Proteins ◽  
Gel Isoelectric Focusing ◽  
Liver Ribosomes

Rat liver ribosomes prepared in low salt buffer contain basic and acidic proteins not found on ribosomes washed in high salt buffer. Proteins extracted from liver ribosomes by 500 mM KCl were characterized by acid urea–polyacrylamide gel electrophoresis, sodium dodecyl sulfate – polyacrylamide gel electrophoresis and gel isoelectric focusing. The salt-solubilized proteins contain 12 polypeptides with a molecular weight over 67 000, several polypeptides with molecular weights less than 67 000, and three polypeptides whose molecular weight exceeded 130 000. Ten to 12 of the proteins were basic, and about 24 acidic proteins were partially or wholly extracted from the ribosomes. Four of the acidic proteins have isoelectric points less than 4.5.

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