Immunoaffinity purification and characterization of thromboxane synthase from porcine lung.

نویسندگان
چکیده

برای دانلود باید عضویت طلایی داشته باشید

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

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Immunoaffinity purification and characterization of thromboxane synthase from porcine lung.

Thromboxane synthase has been purified 620-fold from porcine lung microsomes by a three-step purification procedure including Lubrol-PX solubilization, reactive blue-agarose chromatography, and immunoaffinity chromatography. The purified enzyme exhibited a single protein band (53,000 daltons) on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Rabbit antiserum raised against the purif...

متن کامل

Immunoaffinity purification and characterization of leucine aminopeptidase from human liver.

Leucine aminopeptidase was purified from human liver cytosol to homogeneity, 1538-fold, with a yield of 84.4% by immunoaffinity chromatography. Increases in the activity and the stability of the enzyme were simultaneously observed during the purification procedure, suggesting the presence of some endogenous inhibitor in cytosol. The specific activity and Km value of the enzyme for L-leucine ami...

متن کامل

Isolation and Characterization of Thromboxane Synthase from Human

Thromboxane synthase from human platelets was purified to apparent homogeneity by conventional chromatographic techniques. A 423-fold enrichment over the specific content in the 100,000 x g sediment from platelet homogenates was obtained. The enzyme gave a single band on sodium dodecyl sulfate-gel electrophoresis corresponding to a monomeric molecular weight of 58,800. One heme per polypeptide ...

متن کامل

Comparative purification and characterization of invertebrate muscle glycogen synthase from the porcine parasite Ascaris suum.

Glycogen synthase has been purified from the obliquely striated muscle of the swine parasite Ascaris suum. The muscle contains a concentration of glycogen synthase and glycogen which is 20-fold and 15-fold, respectively, greater than rabbit skeletal muscle. The enzyme could not be solubilized with salivary amylase, but partial solubilization was achieved by activation of endogenous phosphorylas...

متن کامل

Monoclonal antibodies to thromboxane synthase from porcine lung. Production and application to development of a tandem immunoradiometric assay.

Two hybridoma cell lines secreting antibodies against thromboxane synthase of porcine lung were produced. Clone TS1 secretes IgG2a antibody of lower affinity, while clone TS2 secretes IgG1 antibody of higher affinity. Both antibodies (when bound to rabbit anti-mouse IgG-Staphylococcus aureus complex) can immunoprecipitate thromboxane synthase from crude enzyme preparations in an active form sug...

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

ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1986

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)67284-9