Isolation of the hemopexin receptor from human placenta.
نویسندگان
چکیده
منابع مشابه
Isolation and characterization of a folate receptor from human placenta.
While folate binding proteins have been described in serum and a variety of tissues, the function of these proteins is unknown. A particulate folate binding protein from human placenta has been isolated and characterized following solubilization with Triton X-100. The protein was purified 61,000-fold using affinity chromatography on pteroylglutamic acid-Sepharose as the major purification step....
متن کاملThe isolation of adrenal-like steroids from the human placenta.
In previous studies on the isolation of progesterone from placenta, the presence of steroids altered by the NaOH procedure was suspected (1). This was apparently confirmed in the isolation of progesterone from pooled plasma of pregnant women by the presence of progestationally active material other than progesterone when measured by the Hooker-Forbes bioassay (2). A new analysis of placenta was...
متن کاملIsolation and characterization of a mannose-specific endocytosis receptor from human placenta.
A receptor which recognizes glycoproteins bearing terminal mannose residues has been isolated from human placental membranes. Washed membranes were solubilized with buffer containing 1% Triton X-100 and applied to a mannose-Sepharose affinity column. The column was eluted with buffer containing 200 mM mannose and 1% cholate. The major protein eluted exhibited a molecular weight of 175 kDa on so...
متن کاملIsolation and characterization of dipeptidyl peptidase IV from human placenta.
Human placenta is surprisingly rich in post-proline dipeptidyl peptidase activity. Among various cell fractions, microsomes have the highest specific activity. A homogeneous enzyme preparation is obtained in a six-step purification procedure. The final preparation appears homogeneous upon dodecyl sulfate electrophoresis, but analytical isoelectric focussing reveals various active bands with iso...
متن کاملIsolation and characterization of methionine synthetase from human placenta.
The cobalamin-dependent enzyme, methionine synthetase, has been purified approximately 1000-fold to apparent homogeneity from human placenta with a 19% recovery. The final two steps of the purification utilized two different affinity columns. The first was a N5-methyltetrahydrofolate-cystamine-agarose column, and the second was a S-adenosylhomocysteine-agarose column. The enzyme was eluted from...
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: Journal of Biological Chemistry
سال: 1987
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)47465-0