scholarly journals DISCONTINUOUS ELECTROPHORESIS OF PEPSIN AND PEPSINOGEN IN THIN SHEETS OF POLYACRYLAMIDE GEL

1970 ◽  
Vol 18 (12) ◽  
pp. 853-861 ◽  
Author(s):  
LEW CUNNINGHAM ◽  
ELLEN M. RASCH ◽  
ANN L. LEWIS ◽  
RICHARD HEITSCH
Keyword(s):  
Crystal Violet ◽  
Polyacrylamide Gel ◽  
Thin Sheets ◽  
Electrophoretic Separation ◽  
Standard Glass ◽  
Glass Support

Electrophoretic separation of discrete protein bands from solutions of crystalline pepsin or pepsinogen was accomplished in a system incorporating pH discontinuity and using standard, glass microslides to support thin (0.25-mm) sheets of 15% polyacrylamide gel. Adherence of gel films to a glass support during fixation and staining with crystal violet not only prevented distortion of gels as a result of swelling, but also provided preparations that could be readily scanned with a microspectrophotometer. A number of discrete peptide bands were identified from different samples of purified pepsin. Among the several heterogeneous components found in commercially available samples of crystalline pepsinogen, there was a characteristic impurity, the mobility of which was directly comparable to that of pepsin run under the same conditions of electrophoresis. Specific details of methodology are presented.

scholarly journals A VERTICAL MICROSYSTEM FOR DISCONTINUOUS ELECTROPHORESIS OF INSECT TISSUE PROTEINS USING THIN SHEETS OF POLYACRYLAMIDE GEL

1972 ◽  
Vol 20 (5) ◽  
pp. 368-384 ◽  
Author(s):  
ANITA C. BEEN ◽  
ELLEN M. RASCH
Keyword(s):  
Periodic Acid ◽  
Polyacrylamide Gel ◽  
Thin Sheets ◽  
Periodic Acid Schiff ◽  
Sudan Black B ◽  
Tissue Extracts ◽  
Salivary Gland Cells ◽  
Schiff Reaction ◽  
Coomassie Brilliant ◽  
Nonspecific Esterases

Proteins extracted from individual pairs of salivary glands or other larval tissues of Sciara coprophila (Diptera) were separated in a vertical microsystem for discontinuous electrophoresis using thin sheets of polyacrylamide gel cast in multiple layers of varying pore size. After electrophoresis at 150 volts for 40 min, gels were stained ( a) for total proteins with Coomassie brilliant blue, ( b) for glycoproteins with the periodic acid-Schiff reaction, ( c) for lipoproteins with Sudan black B or ( d) for nonspecific esterases with fast blue RR as coupler and α-naphthol acetate as substrate. Sequential application of these reactions to individual gel sectors permitted direct comparisons of protein profiles for 15-20 different samples of tissue extracts carried on a single gel sheet in adjacent lanes and thus subjected to identical conditions of electrophoresis. Representative photographs and densitometric scans are presented to show the suitability of thin gel sheets for autoradiography and for both qualitative and quantitative evaluation of tissue-specific differences in patterns of protein banding found for salivary gland cells, the gastric ceca, or the hemolymph of individual Sciara larvae sacrificed at particular stages of fourth instar development. Innovative details of methodology are presented, including the use of a microspectrophotometer to scan electropherograms of insect proteins and several types of human blood serum.

Enhanced electrophoretic separation of proteins by tethered SiO2 nanoparticles in an SDS-polyacrylamide gel network

The Analyst ◽  
2020 ◽  
Vol 145 (2) ◽  
pp. 415-423 ◽  
Author(s):  
Sayyed Hashem Sajjadi ◽  
Hossein Ahmadzadeh ◽  
Elaheh K. Goharshadi
Keyword(s):  
Gel Electrophoresis ◽  
Heat Dissipation ◽  
Separation Efficiency ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sio2 Nanoparticles ◽  
Polyacrylamide Gel ◽  
Electrophoretic Separation ◽  
Sds Page ◽  
Separation Of Proteins ◽  
Gel Network

Tethered nanoparticles (NPs) are able to improve the separation efficiency of proteins in SDS-polyacrylamide gel electrophoresis (SDS-PAGE) due to their capability of enhancing heat dissipation during electrophoresis and restriction of electrophoretic movement of NPs.

PIGEON CROP SAC-STIMULATING ACTIVITY IN THE PITUITARY OF THE FLOUNDER (PLEURONECTES FLESUS)

1970 ◽  
Vol 47 (4) ◽  
pp. 463-469 ◽  
Author(s):  
A. CHADWICK
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Electrophoretic Separation ◽  
Stimulating Hormone

SUMMARY The examination of a pigeon crop sac-stimulating hormone from flounder pituitaries by polyacrylamide gel electrophoresis is described. Elution of the proteins after electrophoretic separation permitted both the identification of the protein bands responsible for stimulating the crop and a comparison with the prolactin bands from rat and toad pituitaries, as well as from the pituitaries of several other species of fish. The nature of the crop-sac response is discussed and it is suggested that certain features, in particular the absence of fatty granules, indicate a difference between fish and tetrapod prolactin sufficient to warrant the adoption of an alternative name for the fish hormone.

Rapid sodium dodecyl sulfat/polyacrylamide gel electrophoresis of urinary proteins.

1980 ◽  
Vol 26 (11) ◽  
pp. 1588-1590 ◽  
Author(s):  
C Cachera ◽  
C Mizon ◽  
J C Fruchart ◽  
J Mizon ◽  
A Tacquet
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Precipitation Method ◽  
Electrophoretic Separation ◽  
Urinary Proteins ◽  
Special Apparatus ◽  
Separation Of Proteins

Abstract We describe a procedure for the convenient separation of proteins by sodium dodecyl sulfate/polyacrylamide gel electrophoresis of urine from cases of renal disease. A precipitation method that requires no special apparatus was used to concentrate the urinary proteins; for electrophoretic separation we used a commercially supplied polyacrylamide/cellulose gel slab. This method seems to be valuable for investigation of proteinuria; we recommend it for routine use.

Electrophoretic Separation of Serum Lipoproteins in Polyacrylamide Gel

1971 ◽  
Vol 17 (2) ◽  
pp. 111-114 ◽  
Author(s):  
Christopher S Frings ◽  
Lowell B Foster ◽  
Patricia S Cohen
Keyword(s):  
Electrophoretic Mobility ◽  
Molecular Size ◽  
Polyacrylamide Gel ◽  
Electrophoretic Separation ◽  
Polyacrylamide Gels ◽  
Serum Lipoproteins ◽  
Electrophoretic Method ◽  
Sudan Black B

Abstract A method is described for electrophoresing lipoproteins in polyacrylamide gels, in which separations depend both on electrophoretic mobility and molecular size. The sample is prestained with Sudan Black B in a sample gel and then resolved by electrophoresis in a discontinuous pH system consisting of a sample gel, concentrating gel, and separating gel. This method was compared with the paper electrophoretic method of Lees and Hatch [J. Lab. Clin. Med. 61, 518(1963)] and was found to be equally useful in phenotyping lipoproteinemias, with two distinct improvements over paper electrophoretic methods: lipoproteins are more quickly and discretely separated.

Electrophoresis of Fish Myofibrillar Proteins With Sodium-Dodecyl Sulfate-Polyacrylamide Gel

1973 ◽  
Vol 30 (5) ◽  
pp. 706-707 ◽  
Author(s):  
E. A. Childs
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Phosphate Buffer ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Myofibrillar Proteins ◽  
Electrophoretic Separation ◽  
Dodecyl Sulfate

A method for electrophoretic separation of fish myofibrillar proteins is described. After incubation in phosphate buffer containing β-mercaptoethanol, sodium-dodecyl sulfate (SDS), and urea, the proteins are separated by SDS-acrylamide gel electrophoresis.

Demonstration of dopa oxidase activity by purified mammalian superoxide dismutase using polyacrylamide gel electrophoretic separation

AGE ◽  
1978 ◽  
Vol 1 (2) ◽  
pp. 56-59
Author(s):  
Thomas E. Brennan ◽  
Harvey C. Shapiro ◽  
Lee M. Edelstein ◽  
L. Michael Snyder
Keyword(s):  
Superoxide Dismutase ◽  
Oxidase Activity ◽  
Polyacrylamide Gel ◽  
Electrophoretic Separation ◽  
Dopa Oxidase
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