THE SULPHYDRYL CONTENT OF β-LACTOGLOBULIN

1960 ◽  
Vol 38 (3) ◽  
pp. 269-274 ◽  
Author(s):  
A. F. S. A. Habeeb
Keyword(s):  
Sodium Dodecyl Sulphate ◽  
Protein A ◽  
Sodium Dodecyl ◽  
Iodoacetic Acid ◽  
Urea Denaturation ◽  
Denatured Protein ◽  
A Value ◽  
Sulphydryl Groups ◽  
Β Lactoglobulin

The reaction of sulphydryl groups of β-lactoglobulin with N-ethylmaleimide, p-chloromercuribenzoate, and iodoacetic acid has been studied. Using N-ethylmaleimide with native and sodium dodecyl sulphate denatured protein, a value of 2.3 groups of sulphydryl per mole of protein was obtained. A value of 2.15 moles of sulphydryl per mole of protein was obtained from reaction with p-chloromercuribenzoate but lower values were obtained after urea denaturation. The reaction of iodoacetic acid was followed by the determination of residual sulphydryl by the p-chloromercuribenzoate method.

THE SULPHYDRYL CONTENT OF β-LACTOGLOBULIN

1960 ◽  
Vol 38 (1) ◽  
pp. 269-274
Author(s):  
A. F. S. A. Habeeb
Keyword(s):  
Sodium Dodecyl Sulphate ◽  
Protein A ◽  
Sodium Dodecyl ◽  
Iodoacetic Acid ◽  
Urea Denaturation ◽  
Denatured Protein ◽  
A Value ◽  
Sulphydryl Groups ◽  
Β Lactoglobulin

The reaction of sulphydryl groups of β-lactoglobulin with N-ethylmaleimide, p-chloromercuribenzoate, and iodoacetic acid has been studied. Using N-ethylmaleimide with native and sodium dodecyl sulphate denatured protein, a value of 2.3 groups of sulphydryl per mole of protein was obtained. A value of 2.15 moles of sulphydryl per mole of protein was obtained from reaction with p-chloromercuribenzoate but lower values were obtained after urea denaturation. The reaction of iodoacetic acid was followed by the determination of residual sulphydryl by the p-chloromercuribenzoate method.

Solubilization and immunoprecipitation of 125I-labelled antigens from Plasmodium knowlesi schizont-infected erythrocytes using non-ionic, anionic and zwitterionic detergents

Parasitology ◽  
1984 ◽  
Vol 88 (1) ◽  
pp. 27-36 ◽  
Author(s):  
R. J. Howard ◽  
J. W. Barnwell
Keyword(s):  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Plasmodium Knowlesi ◽  
Polyacrylamide Gel Electrophoresis ◽  
Protein A ◽  
Sodium Dodecyl ◽  
Ionic Detergents ◽  
Class A ◽  
Anionic Detergents ◽  
Triton X

SUMMARYPlasmodium knowlesi malaria-infected erythrocytes were radio-iodinated and several non-ionic, anionic and zwitterionic detergents were compared in their capacity to extract the labelled membrane proteins. The use of these detergents for antigen identification was tested by immunoprecipitation, after addition of Triton X-100 to some detergent extracts, using hyperimmune monkey antiserum and protein A-Sepharose. 125I-labelled antigens were specifically immunoprecipitated with all detergents tested, including the anionic detergents sodium dodecyl sulphate (SDS), deoxycholate and cholate; the zwitterions Zwittergent-312 and -314, CHAPS and Empigen BB, as well as several non-ionic detergents. The SDS-polyacrylamide gel electrophoresis patterns of 125I-labelled antigens varied after extraction with different detergents, there being no consistent pattern for detergents of a particular class. A total of 14 125I-labelled antigens were identified, 11 of them using Triton X-100. Some minor antigens identified with Triton X-100 were immunoprecipitated in greater amount after extraction in other detergents. Most importantly, two antigens Mr 200000 and 180000 were detected only after extraction with deoxycholate or SDS.

scholarly journals The molecular size of N-methylglutamate dehydrogenase of Pseudomonas aminovorans

1977 ◽  
Vol 167 (2) ◽  
pp. 509-512 ◽  
Author(s):  
C W Bamforth ◽  
P J Large
Keyword(s):  
Molecular Weight ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Protein A ◽  
Sodium Dodecyl ◽  
Molecular Size ◽  
Partial Specific Volume ◽  
Triton X

N-Methylglutamate dehydrogenase, purified to a specific activity of 0.29 unit/mg of protein, gave one band on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, corresponding to a molecular weight of 130 000. Enzyme-Triton complexes were found to have a partial specific volume of 0.73 cm3/g, suggesting that the protein binds less than 0.1 g of Triton/g of protein. A molecular weight for the intact enzyme in the presence of 1% (w/v) Triton X-100 of 550 000 suggested that the enzyme may be a tetramer.

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