Protein phosphorylation in rat liver plasma membranes
نویسندگان
چکیده
منابع مشابه
Plasma Membranes of the Rat Liver
A method is described for the rapid isolation of a plasma membrane fraction containing a high concentration of intact bile canaliculi from the rat liver. Isolated bile canaliculi retain most of the ultrastructural features exhibited in the intact liver cell. The final fraction contains 5'-nucleotidase activity at approximately the same concentration as that in previous preparations of plasma me...
متن کاملIsolation of Rat Liver Plasma Membranes
Nucleotide pyrophosphatase and phosphodiesterase I of rat liver have been found to be localized primarily in cell particulates highly enriched with respect to the most commonly accepted plasma membrane marker, 5'-nucleotidase, and therefore should themselves be assigned a plasma membrane localization. The observation that plasma membranes sediment in isotonic sucrose with both nuclear and micro...
متن کاملAlkaline ribonuclease and phosphodiesterase activity in rat liver plasma membranes.
The ribonuclease and phosphodiesterase activities of rat liver plasma membranes, purified from the crude nuclear fraction by centrifugation in an A-XII zonal rotor and flotation, were examined and compared. The plasma membrane is responsible for between 65 and 90% of the phosphodiesterase activity of the cell and between 25 and 30% of the particulate ribonuclease activity measured at pH8.7 in t...
متن کاملIsolation and partial characterization of a fatty acid binding protein in rat liver plasma membranes.
When [14C]oleate-bovine serum albumin complexes were incubated in vitro with rat liver plasma membranes (LPM), specific, saturable binding of oleate to the membranes was observed. Maximal heat-sensitive (i.e., specific) binding was 3.2 nmol/mg of membrane protein. Oleate-agarose affinity chromatography of Triton X-100-solubilized LPM was used to isolate a single 40-kDa protein with high affinit...
متن کاملras proteins enhance the phosphorylation of a 38 kDa protein (p38) in rat liver plasma membrane.
Phosphorylation of a 38 kDa protein (p38) present in rat liver plasma membrane has been shown for the first time to be enhanced by ras proteins. This increase in phosphorylation is about 3-16-fold depending on the incubation time and the type of ras protein used. Acid treatment removes phosphate from this protein suggesting that the phosphorylation involves phosphoramidate derivatives of basic ...
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: FEBS Letters
سال: 1980
ISSN: 0014-5793
DOI: 10.1016/0014-5793(80)80630-2