Purification and characterization of calcyclin from human placenta.
نویسندگان
چکیده
منابع مشابه
PARTIAL PURIFICATION AND PROPERTIES OF L-GLUTAMINE: D-FRUCTOSE 6-P AMIDOTRANSFERASE FROM HUMAN PLACENTA
The first enzyme of the pathway for uridine diphosphate N-acetyl-D-glucosamine (UDPAG) biosynthesis i.e. L-glutamine: D-fructose 6-P amidotransferase (E.C. 2.6.1.16) was purified 52-fold from human placenta using methanol fractionation and column chromatography on DEAE-Sephadex A-50. The enzyme showed optimal activity in a broad range of pH from 5.8 to 7.8 in both phosphate and cacodylate ...
متن کاملPurification and partial characterization of lipoxygenase with dual catalytic activities from human term placenta.
Lipoxygenase possessing dual catalytic activities, i.e. dioxygenase and hydroperoxidase, was purified from the cytosols of term placentas from non-smoking women. Concanavalin A affinity chromatography followed by phenyl-Sepharose CL-4B chromatography resulted in the separation of one hydrophobic and one non-hydrophobic isoenzyme. The concanavalin A-purified enzyme was used in all subsequent exp...
متن کاملPurification and properties of glutathione peroxidase from human placenta.
Glutathione peroxidase (glutathione--H2O2 oxidoreductase; EC 1.11.1.9) was purified to homogeneity from human placenta by using (NH4)2SO4 precipitation, ion-exchange chromatography, Sephadex gel filtration and preparative polyacrylamide-disc-gel electrophoresis. Glutathione peroxidase from human placenta is a tetramer, having 4g-atoms of selenium/mol of protein. The molecular weight of the enzy...
متن کاملPurification and properties of steroid sulfatase from human placenta.
Steroid sulfatase was purified approximately 170-fold from normal human placental microsomes and properties of the enzyme were investigated. The major steps in the purification procedure included solubilization with Triton X-100, column chromatofocusing, and hydrophobic interaction chromatography on phenylsepharose CL-4B. The purified sulfatase showed a molecular weight of 500-600 kDa on HPLC g...
متن کامل[Purification and characterization of the membrane associated calmodulin from the human placenta].
The protein with the most predominant Ca2+ binding activity in membrane fractions of the human placenta was purified to electrophoretical homogeneity. This protein was identified as the membrane bound form of calmodulin based on the immunological cross reactivity and a number of biochemical properties. The membrane fraction of the human placenta contained 8.3% of the total cellular calmodulin a...
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: Japanese Journal of Pharmacology
سال: 1991
ISSN: 0021-5198
DOI: 10.1016/s0021-5198(19)38666-4