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.

ISOLATION OF HIGHLY PURIFIED SEX HORMONE BINDING GLOBULIN (SHBG): EVIDENCE FOR MICROHETEROGENEITY

1979 ◽  
Vol 90 (4) ◽  
pp. 737-742 ◽  
Author(s):  
W. Mischke ◽  
H. C. Weise ◽  
D. Graesslin ◽  
R. Rusch ◽  
J. Tamm
Keyword(s):  
Human Serum ◽  
Isoelectric Focusing ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Double Diffusion ◽  
Polyacrylamide Gel ◽  
Sex Hormone ◽  
Sex Hormone Binding Globulin ◽  
Hormone Binding ◽  
Gel Isoelectric Focusing

ABSTRACT Highly purified sex hormone binding globulin (SHBG) was isolated in milligram amounts from a human serum fraction (Cohn IV-4). The final preparation was homogeneous by the criteria of polyacrylamide-gel electrophoresis. Immunological evidence for purity could be given by double diffusion according to Ouchterlony. However, following gel isoelectric focusing highly purified SHBG displayed four different bands, as could be demonstrated by staining as well as by a photoscan of the [3H]5α-dihydrotestosterone-SHBG complex. After incubation with neuraminidase the microheterogeneity of SHBG disappeared and the asialo-SHBG showed only one band.

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