Conformational study and determination of the molecular weight of highly charged basic proteins by sedimentation equilibrium and gel electrophoresis

Biochemistry ◽  
1982 ◽  
Vol 21 (23) ◽  
pp. 5910-5918 ◽  
Author(s):  
Juan Ausio ◽  
Juan A. Subirana
1990 ◽  
Vol 10 (2) ◽  
pp. 131-139
Author(s):  
Oyewole Adeyemo ◽  
E. O. Okegbile ◽  
O. O. Olorunsogo

For the development of immunological contraception, attention is being concentrated on the possibility of using a sperm membrane antigen. Boar sperm membrane was extracted with triton-X 100 and fractionated by Sephadex G-150 column chromatography. The glycosylated and nonglycosylated portions of protein peaks from the gel filtration were obtained by fractionating on concanavalin A-Sepharose and eluting the bound protein with 0.3 M methyl mannoside. A glycosylated fraction was found to induce sperm agglutinating antibodies in rabbit. The partially purified protein has a molecular weight of 30 kilodaltons, as determined by sodium dodecyl polyaccyrlamide gel electrophoresis. Further work is planned on the histochemical determination of the origin of this protein and species cross-activity of the antibody.


1969 ◽  
Vol 115 (4) ◽  
pp. 639-643 ◽  
Author(s):  
R. H. Villet ◽  
K. Dalziel

A method is described for the isolation of 6-phosphogluconate dehydrogenase from sheep liver. The product appears to be homogeneous in polyacrylamide-gel electrophoresis and in sedimentation-velocity and sedimentation-equilibrium studies in the ultracentrifuge. The molecular weight is estimated as 129000 from equilibrium sedimentation.


1988 ◽  
Vol 9 (12) ◽  
pp. 803-806 ◽  
Author(s):  
Hideyuki Nishizawa ◽  
Natsumi Kita ◽  
Sakiko Okimura ◽  
Emi Takao ◽  
Yoshihiro Abe

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