The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis.
نویسندگان
چکیده
Forty proteins with polypeptide chains of well characterized molecular weights have been studied by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate following the procedure of Shapiro, Vifiuela, and Maize1 (Biochem. Biophys. Res. Commun., 28, 815 (1967)). When the electrophoretic mobilities were plotted against the logarithm of the known polypeptide chain molecular weights, a smooth curve was obtained. The results show that the method can be used with great confidence to determine the molecular weights of polypeptide chains for a wide variety of proteins.
منابع مشابه
Purification and properties of an NADP-specific 6-phosphogluconate dehydrogenase from Streptococcus faecalis.
A procedure is described for the purification of 6-phosphogluconate dehydrogenase (6-phospho-D-gluconate:NADP oxidoreductase (decarboxylating) EC 1.1.1.44) from cell extracts of Streptococcus gaecalis. A 180-fold purification was achieved with an over-all yield of about 12% and an average specific activity of 14. The enzyme was homogeneous as determined by polyacrylamide gel electrophoresis, im...
متن کاملInternal standards for molecular weight determinations of proteins by polyacrylamide gel electrophoresis. Applications to envelope proteins of Escherichia coli.
A new technique was devised to be used with molecular weight determinations of proteins on polyacrylamide gels. Internal standards consisting of proteins covalently linked to l-dimethylaminonaphthalene-S-sulfonyl(DANS-) groups were prepared. DANSderivatives of insulin and monomer, dimer, trimer, tetramer, pentamer, and hexamer of egg white lysozyme and serum albumin covered molecular weights fr...
متن کاملPurification of horse serum cholinesterase by preparative polyacrylamide gel electrophoresis.
Preparative polyacrylamide gel electrophoresis has been used in the final stages of purification to prepare horse serum cholinesterase which was at least 9.5% pure, as judged by analytical polyacrylamide gel electrophoresis. The starting material, already purified about 109-fold by the Strelitz method, was purified an additional 89-fold by the procedure. The method involved Sephadex G-ZOO and S...
متن کاملPurification and properties of beta-N-acetylglucosaminidase from Escherichia coli.
beta-N-acetylglucosaminidase (EC 3.2.1.30) has been purified from Escherichia coli K-12 to near homogeneity based on polyacrylamide gel electrophoresis in both 0.5% sodium dodecyl sulfate and in 6 M urea at pH 8.5. The purified enzyme shows a pH optimum of 7.7 and the Km for p-nitrophenyl-beta-D-2-acetamido-2-deoxyglucopyranoside is 0.43 mM. The molecular weight of this enzyme, determined by bo...
متن کاملPurification and properties of Clostridium botulinum type F toxin.
Clostridium botulinum type F toxin of proteolytic Langeland strain was purified. Toxin in whole cultures was precipitated with (NH4)2SO4. Extract of the precipitate was successively chromatographed on diethylaminoethyl-cellulose at pH 6,0, O-(carboxymethyl) cellulose at pH 4.9, and finally diethylaminoethyl-cellulose at pH 8.1. The procedure recovered 14 percent of the toxin assayed in the star...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 244 16 شماره
صفحات -
تاریخ انتشار 1969