Effect of fatty acids on the movement and staining of membrane proteins in polyacrylamide gel electrophoresis

1972 ◽  
Vol 46 (3) ◽  
pp. 1347-1353 ◽  
Author(s):  
June M. Fessenden-Raden
Keyword(s):  
Fatty Acids ◽  
Membrane Proteins ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel

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

Compositional and electrophoretic changes in buffalo milk-fat globule membrane proteins during lactation

1976 ◽  
Vol 43 (3) ◽  
pp. 381-388 ◽  
Author(s):  
Sukhminder Singh ◽  
N. C. Ganguli
Keyword(s):  
Membrane Proteins ◽  
Isoelectric Focusing ◽  
Gel Electrophoresis ◽  
Milk Fat ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Milk Fat Globule Membrane ◽  
Milk Fat Globule ◽  
Fat Globule

SummaryChemical analyses, polyacrylamide-gel electrophoresis and isoelectric focusing of milk-fat globule membrane proteins (FGMP) obtained from the milk of 2 Murrah buffaloes were done to determine if any change in composition occurred during lactation. Changes in the levels of sialic acid, hexose, hexosamine, N and P were found in the FGMP obtained at different stages of lactation. On the day of parturition, 8 major proteins in FGMP were determined by sodium dodecyl sulphate polyacrylamide-gel electrophoresis whereas 6 major proteins were obtained in FGMP of middle and late lactation milks. Isoelectric focusing of FGMP showed 8–9, 9–13 and 13–16 proteins from colostrum, middle and late lactation milks, respectively and the isoelectric pH of the proteins varied from 5·25 to 7·80, 5·85 to 8·30 and 5·75 to 8·61 respectively.

scholarly journals Membrane proteins of chromaffin granules. Dopamine β-hydroxylase, a major constituent

1972 ◽  
Vol 129 (1) ◽  
pp. 187-195 ◽  
Author(s):  
Heide Hörtnagl ◽  
H. Winkler ◽  
H. Lochs
Keyword(s):  
Membrane Proteins ◽  
Gel Electrophoresis ◽  
Cetylpyridinium Chloride ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Major Constituent ◽  
Chromaffin Granules ◽  
Lower Mobility ◽  
Membrane Bound ◽  
Immunological Cross Reaction

1. Soluble lysates and membranes were prepared from chromaffin granules isolated from bovine adrenal medulla. The detergent N-cetylpyridinium chloride was used for solubilizing the membrane proteins, including the membrane-bound dopamine (2,4-dihydroxyphenethylamine) β-hydroxylase. The solubilized proteins were fractionated by Sephadex chromatography in the presence of N-cetylpyridinium chloride. The major component of the membrane proteins, i.e. chromomembrin A, was identified as the enzyme dopamine β-hydroxylase. 2. The addition of N-cetylpyridinium chloride to the soluble lysate caused precipitation of up to 96% of the proteins, but only a small proportion of the dopamine β-hydroxylase activity was precipitated. The only protein demonstrable in the supernatant by polyacrylamide-gel electrophoresis was the protein that has a lower mobility than chromogranin A in disc gel electrophoresis. This component has been identified previously as dopamine β-hydroxylase. Thus, this method provides an extremely simple isolation procedure for dopamine β-hydroxylase. 3. A comparison of the membrane-bound and soluble dopamine β-hydroxylases revealed the identity of these two preparations. Both were activated by N-cetylpyridinium chloride, they migrated identically in polyacrylamide-gel electrophoresis, their amino acid composition was very similar and an immunological cross-reaction could be demonstrated.

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