Purification and characterization of a lysophosphatidic acid-specific phosphatase
نویسندگان
چکیده
منابع مشابه
Purification and Characterization of a Potato Tuber Acid Phosphatase Having Significant Phosphotyrosine Phosphatase Activity.
The major acid phosphatase (APase) from potato (Solanum tuberosom L. cv Chiefton) tubers has been purified 2289-fold to near homogeneity and a final O-phospho-L-tyrosine (P-Tyr) hydrolyzing specific activity of 1917 [mu]mol Pi produced min-1 mg-1 of protein. Nondenaturing polyacrylamide gel electrophoresis of the final preparation resolved a single protein-staining band that co-migrated with AP...
متن کاملProstatic acid phosphatase degrades lysophosphatidic acid in seminal plasma.
Lysophosphatidic acid (LPA) is a lipid mediator with multiple biological activities and is detected in various biological fluids, including human seminal plasma. Due to its cell proliferation stimulatory and anti-apoptotic activities, LPA has been implicated in the progression of some cancers such as ovarian cancer and prostate cancer. Here, we show that prostatic acid phosphatase, which is a n...
متن کاملPurification and characterization of a novel protein phosphatase highly specific for ribosomal protein S6.
Ribosomal protein S6 is the principal phosphoprotein of the eucaryotic ribosome that becomes multiply phosphorylated on serine residues in response to a wide variety of mitogenic stimuli. In this paper the principal protein phosphatases able to dephosphorylate S6 were characterized in Xenopus laevis ovary and eggs. Two enzymes termed peak I and peak II were found to account for most S6 phosphat...
متن کاملIsolation of lysophosphatidic acid phosphatase from developing peanut cotyledons.
The soluble fraction of immature peanut (Arachis hypogaea) was capable of dephosphorylating [(3)H]lysophosphatidic acid (LPA) to generate monoacylglycerol (MAG). The enzyme responsible for the generation of MAG, LPA phosphatase, has been identified in plants and purified by successive chromatography separations on octyl-Sepharose, Blue Sepharose, Superdex-75, and heparin-agarose to apparent hom...
متن کاملPurification and characterization of a low molecular weight acid phosphatase from bovine liver.
Several mammalian tissues have been shown to contain as many as three acid phosphatases which may be separated on the basis of differences in size by gel filtration on Sephadex G-75. The smallest of these enzymes from bovine liver, termed acid phosphatase III, has been purified to apparent homogeneity. The purified enzyme migrates as a single band during electrophoresis on polyacrylamide gel an...
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: Biochemical Journal
سال: 1998
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj3360483