Vertical Plate Gel Electrophoresis for the Differentiation of Meat Species

1972 ◽  
Vol 55 (3) ◽  
pp. 461-463
Author(s):  
R J Coduri ◽  
A G Rand
Keyword(s):  
Gel Electrophoresis ◽  
Muscle Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Meat Products ◽  
Single Species ◽  
Direct Analysis ◽  
Buffer System ◽  
Mixed Species ◽  
Detection And Identification ◽  
Meat Proteins

Abstract Polyacrylamide gel electrophoresis of fresh meat sarcoplasmic proteins by the vertical plat e technique was studied as a method for the detection and identification of pure and mixed species extracts. A single 7% Cyanogum gel containing 1M urea, in conjunction with a tris-chloride, tris-glycine discontinuous buffer system, produced satisfactory resolution of single species and mixed species muscle protein extracts. Eleetrophoretie patterns were obtained by direct analysis of meat proteins extracted with a tris-chloride-10% glucose extraction buffer at pH 6.7. Mixtures of beef and pork and beef and horse were easily identified. The possibility for a d a p t i n g t h e eleetrophoretie procedure to the analysis of cooked meat products and non-meat proteins is discussed.

Vertical Plate Gel Electrophoresis for the Differentiation of Fish and Shellfish Species

1972 ◽  
Vol 55 (3) ◽  
pp. 464-466
Author(s):  
R J Coduri ◽  
A G Rand
Keyword(s):  
Gel Electrophoresis ◽  
Vertical Plate ◽  
Polyacrylamide Gel Electrophoresis ◽  
Direct Analysis ◽  
Buffer System ◽  
Electrophoretic Patterns ◽  
Extraction Buffer ◽  
Frozen Fish ◽  
Fish And Shellfish ◽  
Electrophoresis Technique

Abstract The vertical plate polyacrylamide gel electrophoresis technique described for differentiation of meat was applied to fresh and frozen fish and shellfish species. A single 7% Cyanogum gel containing mercaptoethanol, in conjunction with a tris-chloride, tris-glycine discontinuous buffer system, produced satisfactory resolution of fish and shellfish species extracts. The electrophoretic patterns were obtained by direct analysis of the proteins extracted with a tris-chloride-10% glucose extraction buffer at pH 6.7. This technique can also be used to detect substitution of one fish or shellfish species for another.

A novel Bicine running buffer system for doubled sodium dodecyl sulfate – polyacrylamide gel electrophoresis of membrane proteins

2006 ◽  
Vol 27 (14) ◽  
pp. 2984-2995 ◽  
Author(s):  
Taufika Islam Williams ◽  
Jennifer C. Combs ◽  
Anup P. Thakur ◽  
Herbert J. Strobel ◽  
Bert C. Lynn
Keyword(s):  
Membrane Proteins ◽  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Buffer System ◽  
Dodecyl Sulfate

scholarly journals Isolation of Some Platelet Membrane Glycoproteins

1977 ◽  
Author(s):  
K.J. Clemetson ◽  
S.L. Pfueller ◽  
A. Sturk ◽  
E.F. Lüscher ◽  
C.S.P. Jenkins
Keyword(s):  
Gel Electrophoresis ◽  
Wheat Germ ◽  
Lens Culinaris ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Platelet Membrane ◽  
Buffer System ◽  
Membrane Glycoproteins ◽  
Abrus Precatorius ◽  
Differential Binding

The platelet is surrounded by a pronounced glycocalix formed by carbohydrate moieties of the membrane glycoproteins. The number of glycoproteins of the outer platelet membrane is greater in number than had previously been reported : when solubilized membranes are analyzed by SDS-polyacrylamide gel electrophoresis the number of separated carbohydrate entities was found not only to be dependant on the concentration of acrylamide and of bisacrylamide used but also on the buffer system employed.The major platelet membrane glycoproteins have been solubilized and subjected to affinity chromatography on the lectins from Lens culinaris, wheat germ and Abrus precatorius. SDS-polyacrylamide gel electrophoresis in the presence and absence of a reducing agent together with the differential binding of the lectins to the glycoproteins permitted the distinction of at least seven glycoprotein entities. Using combinations of lectin columns, two platelet membrane glycoproteins have been isolated and others have been greatly purified.

scholarly journals Immunochemical studies on Tn erythrocyte glycoprotein

Blood ◽  
1981 ◽  
Vol 58 (6) ◽  
pp. 1228-1231 ◽  
Author(s):  
LT Lee ◽  
S Frank ◽  
DS de Jongh ◽  
C Howe
Keyword(s):  
Influenza Virus ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Direct Analysis ◽  
Polyacrylamide Gel ◽  
Salvia Sclarea

Abstract Glycoproteins were extracted from membranes of erythrocytes that displayed Tn polyagglutination and were compared chemically and immunologically with glycoproteins of group O, MN cells. Tn glycoprotein had lower than normal NANA : protein and sugar : protein ratios, as revealed by direct analysis and polyacrylamide gel electrophoresis, and displayed slower immunoelectrophoretic mobility than glycoproteins of group O, MN cells. Agglutination of Tn cells by Salvia sclarea lectin was inhibited by Tn glycoprotein but not by O, MN glycoprotein. Tn and MN glycoproteins were equally potent inhibitors of influenza virus HA. Our findings indicate than Tn-specific determinants are part of the glycophorin molecule.

scholarly journals Multiple forms of acetylcholinesterase from pig brain

1973 ◽  
Vol 133 (4) ◽  
pp. 655-665 ◽  
Author(s):  
Christopher H. S. McIntosh ◽  
David T. Plummer
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Buffer System ◽  
Soluble Enzyme ◽  
Molecular Weights ◽  
Pig Brain ◽  
Spacer Gel ◽  
Solubilized Enzyme ◽  
Triton X

1. A number of methods of solubilization of pig brain acetylcholinesterase (EC 3.1.1.7) were studied. The multiple enzymic forms of the resultant preparations were examined by polyacrylamide-gel electrophoresis. 2. Butanol extraction, Nagarase treatment and ultrasonication proved unsuitable as preparatory methods, but detergent treatment (Triton X-100, Triton X-100–KCl and lysolecithin) gave good yields. 3. Separation of soluble enzyme in three systems of polyacrylamide-gel electrophoresis were compared and the relative advantages are discussed. 4. By using a 6% (w/v) gel and continuous buffer system two forms of acetylcholinesterase were detected in Triton X-100-solubilized enzyme, but the incorporation of a sample and spacer gel and a discontinuous buffer system resolved this into four components. The forms of the soluble enzyme extracted by different methods differed in mobility. 5. With gradient polyacrylamide-gel electrophoresis between two and six forms were detected, depending on the method used for extraction. The average molecular weights of the five forms most frequently found were 60000, 130000, 198000, 266000 and 350000. 6. Treatment of the Triton X-100-extracted enzyme with 2.5m-urea altered the pattern and evidence of dissociation was observed. 7. The results are discussed in the light of present theories on the molecular structure of acetylcholinesterase.

Collagen deficiency and ruptured cerebral aneurysms

1983 ◽  
Vol 59 (1) ◽  
pp. 16-20 ◽  
Author(s):  
Glenn Neil-Dwyer ◽  
John R. Bartlett ◽  
Alan C. Nicholls ◽  
Paolo Narcisi ◽  
F. Michael Pope
Keyword(s):  
Gel Electrophoresis ◽  
Matched Control ◽  
Polyacrylamide Gel Electrophoresis ◽  
Cerebral Aneurysms ◽  
Surgical Patients ◽  
Buffer System ◽  
Type Iii Collagen ◽  
Content Type ◽  
Type Iii ◽  
And Control

✓ Skin and temporal arterial biopsies were obtained from 17 patients undergoing surgery for ruptured cerebral aneurysm, and specimens were taken from six age- and sex-matched control surgical patients. Radioactively labeled and control tissue collagen patterns were studied by interrupted polyacrylamide gel electrophoresis (PAGE), using the trisborate buffer system or by carboxymethyl cellulose (CMC) chromatography. Type III/I collagen ratios were then measured from autoradiographs of the radioactively labeled samples using the Joyce Loebl gel scanner adapted for flat bed gels. In the case of the CMC labeled material, the ratios were measured by the ratios of the summed radioactively labeled α1(III), α2(II), and α2(I) peaks. Eleven of the 17 patients were Type III collagen-deficient while all of the six control patients had normal collagen ratios. The implications of these findings are discussed.

scholarly journals Dodecyl sulphate/polyacrylamide-gel electrophoresis at low pH values and low temperatures

1979 ◽  
Vol 181 (3) ◽  
pp. 759-761 ◽  
Author(s):  
R Lichtner ◽  
H U Wolf
Keyword(s):  
Low Temperatures ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Catalyst System ◽  
Low Ph ◽  
Polyacrylamide Gel ◽  
Buffer System ◽  
Simple Method ◽  
Ph Values

A simple method is described for dodecyl sulphate/polyacrylamide-gel electrophoresis of pH- and temperature-labile biological intermediates. The method is based on a catalyst system that works at temperatures of 2–4 degrees C and pH values of 2–4 and an appropriate buffer system containing Li+ or Tris [CH2OH–C(CH2OH)2–NH3+] instead of Na+. This system does not lead to the precipitation of 1% dodecyl sulphate.

Test to Determine Whether Shucked Oysters Have Been Frozen and Thawed

1970 ◽  
Vol 53 (6) ◽  
pp. 1237-1241 ◽  
Author(s):  
Edith Gould ◽  
Michael J Medler
Keyword(s):  
Enzyme Activity ◽  
Gel Electrophoresis ◽  
Malic Enzyme ◽  
Polyacrylamide Gel Electrophoresis ◽  
Histochemical Staining ◽  
Soluble Form ◽  
Buffer System ◽  
Freezing And Thawing ◽  
Bacterial Action ◽  
Malic Enzyme Activity

Abstract An objective test is described that will detect whether refrigerated, shucked whole oysters have been frozen and thawed at any time. Latent forms of malic enzyme activity are solubilized by freezing and thawing and can be differentiated from the normally soluble form by their differing rates of electrophoretic migration under the conditions described in this paper. SuperchiUed (23°F) oyster meats showed the same latent malic enzyme activity as the frozen. A sharply discontinuous buffer system during the polyacrylamide gel electrophoresis and a carefully timed incubation period for the histochemical staining are essential to the test. In oyster meats stored at 34°F for up to 3 weeks, neither autolysis nor bacterial action was great enough to produce the enzymogram peculiar to oysters that have been frozen or superchilled and thawed.

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