Structural Properties of Bovine Brain S-100 Protein
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چکیده
منابع مشابه
Distribution of immunoreactive S-100 protein in pediatric brain tumors.
The distribution of S-100 proteins was examined in 98 pediatric brain neoplasms with rabbit antiserum to S-100 protein, utilizing the peroxidase-antiperoxidase (PAP) immunohistochemical technique. Positive cytoplasmic immunoreactivity was present in 22 of 24 astrocytomas, both oligodendrogliomas, eight of 13 ependymomas, all 11 choroid plexus tumors, all nine schwannomas, two of six meningiomas...
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The single tyrosine residue in S-100b protein was nitrated by treatment with tetranitromethane in 0.1 M-Tris/HCl buffer, pH 8.0, containing 2 mM-EDTA. The nitrated protein did not differ significantly in secondary structure from its native unmodified counterpart, as revealed by far-u.v. c.d. measurements. The effect of Ca2+ on the modified protein was different from that on the native protein, ...
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S100 proteins were first discovered in 1965 by Moore as a major protein fraction (0.6% of total soluble protein) isolated from bovine brain (Moore 1965). The protein was given the name S100 due to its high solubility in saturated ammonium sulfate. Later experiments showed the S100 protein fraction constituted two different dimeric species comprised of two b protomers (S100B) or an a, b heterodi...
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S100P protein consists of 95 amino acids with a molecular weight of 10.4 kDa. S100P is a Ca binding protein that belongs to S100 family ("Soluble in 100% saturated solution with ammonium sulfate") which was first isolated from human placenta and is therefore designated as "P". S100 family includes at least 26 members, which are thought to be expressed only in vertebrates and are present in a ti...
متن کاملOptical and Nano structural properties of Hematite (α-Fe2O3) nanorods in interaction with Bovine Serum Albumin (BSA) Protein Solution
Hematite (α-Fe2O3) nanorods were synthesized by hydrothermal method using Cetyltrimethylammonium bromide (CTAB) as a surfactant agent. To study optical, nanostructural properties, and to control the morphology and shape of nanorods, 0.025 mol L-1, 0.05 mol L-1 and 0.1 mol L-1 concentration of CTAB were used. Moreover, the effect of interaction between bovine serum albumin (BSA) A9418-5G protein...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1971
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)61785-5