Purification of Retinal 5-Antigen to Homogeneity by the Criterion of Gel Electrophoresis Silver Staining

نویسندگان

  • J. Samuel Zigler
  • Manabu Mochizuki
  • Toichiro Kuwabara
چکیده

This report describes a procedure by which high performance liquid chromatographic (HPLC) techniques are used to obtain homogeneous S-antigen. Conventionally prepared S-antigen was purified further by fractionation on the anion exchange Mono-Q column followed by gel filtration on a TSK-3000 column. This procedure produced an S-antigen preparation, which appeared homogeneous by gel electrophoresis using the very sensitive silver staining method. The purified material retained its immunochemical and uveitogenic activity. The availability of homogeneous S-antigen will facilitate studies aimed at elucidating, at the molecular level, the mechanism by which S-antigen induces uveitis. Invest Ophthalmol Vis Sci 25:977-980, 1984

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Purification of retinal S-antigen to homogeneity by the criterion of gel electrophoresis silver staining.

This report describes a procedure by which high performance liquid chromatographic (HPLC) techniques are used to obtain homogeneous S-antigen. Conventionally prepared S-antigen was purified further by fractionation on the anion exchange Mono-Q column followed by gel filtration on a TSK-3000 column. This procedure produced an S-antigen preparation, which appeared homogeneous by gel electrophores...

متن کامل

Purification and characterization of mitochondrial imidazoline-guanidinium receptive site from rabbit kidney.

The imidazoline-guanidinium receptive site (IGRS) is a membrane-bound protein that may mediate some of the pharmacological effects of imidazoline and guanidinium compounds. The structure and functionality of this protein are unknown but, in addition to its location at the plasma membrane, it is found in high density in the outer membrane of mitochondria (Tesson, F., Prip-Buus, C., Lemoine, A., ...

متن کامل

Purification of murine erythropoietin produced in serum-free cultures of erythroleukemia cells.

We previously documented that several erythroleukemia cell lines released factors that stimulated erythropoiesis in vivo and in vitro. A simple five-step scheme has been devised that allows purification of this erythropoietic activity to apparent homogeneity. The methods employed included lectin affinity chromatography (wheat germ agglutinin), gel filtration (ultro gel ACA44), ion exchange, hyd...

متن کامل

Purification of an active opioid-binding protein from bovine striatum.

We report the purification to apparent homogeneity of an active opioid-binding protein solubilized from bovine striatal membranes. The purification was accomplished in two steps: affinity chromatography on beta-naltrexylethylenediamine (NED)-CH-Sepharose 4B followed by lectin affinity chromatography on wheat germ agglutinin-agarose. The ligand affinity-purified fraction exhibits stereospecific ...

متن کامل

Purification to apparent homogeneity and partial amino acid sequence of rat liver O6-alkylguanine-DNA-alkyltransferase

O6-alkylguanine-DNA-alkyltransferase (ATase) activity was increased in rat liver from 80 to 320 fmoles/mg total protein 48 h after administration of 2-acetylaminofluorene at 60 mg/kg body weight. This tissue was used as a source of ATase which was purified by ammonium sulphate precipitation and DNA-cellulose, molecular exclusion and ion exchange chromatography (IEC). IEC purified material showe...

متن کامل

ذخیره 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 نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2005