Identification, immunoaffinity purification and partial characterization of a human decidua-associated protein
نویسندگان
چکیده
منابع مشابه
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 کاملHigh-Level Expression, Single-Step Immunoaffinity Purification and Characterization of Human Tetraspanin Membrane Protein CD81
The study of membrane protein structure and function requires their high-level expression and purification in fully functional form. We previously used a tetracycline-inducible stable mammalian cell line, HEK293S-TetR, for regulated high-level expression of G-protein coupled receptors. We here report successfully using this method for high-level expression of de novo oligo-DNA assembled human C...
متن کاملHuman platelet basic protein associated with antiheparin and mitogenic activities: purification and partial characterization.
Platelet basic protein (PBP) (isoelectric point, 10.0-10.5; apparent Mr, 11,000-15,000) has been purified to homogeneity from material secreted by fresh human platelets after stimulation by thrombin. The purification, using preparative isoelectric focusing and chromatography on heparin-Sepharose, yielded two additional peptides with antiheparin activity that were immunologically identical with ...
متن کاملPurification and partial characterization of a murine melanoma-associated antigen.
A murine B16 melanoma-associated antigen was detected and partially purified from spent culture medium and intracellular material. The antigen was also purified and partially characterized from the detergent extract of cells cultured in the presence of [3H]glucosamine done or together with [‘4C]leucine. During purification, the melanoma-associated antigen activity was monitored by a double anti...
متن کاملIdentification, partial purification, and characterization of a novel phospholipid-dependent and fatty acid-activated protein kinase from human platelets.
A novel lipid-dependent protein kinase in human platelets was partially purified and characterized. This enzyme was calcium-independent and was selective for phosphatidic acid as a cofactor/activator with initial activation observed at approximately 2 mol % and peak activity achieved at 4 mol % phosphatidic acid. In the presence of phosphatidylserine, enzyme activation was observed with concent...
متن کاملذخیره 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: Reproduction
سال: 1990
ISSN: 1470-1626,1741-7899
DOI: 10.1530/jrf.0.0880159