PROPERTIES OF A RAT SERUM-PROTEIN LABELED BY INJECTION OF SODIUM SELENITE
PROPERTIES OF A RAT SERUM-PROTEIN LABELED BY INJECTION OF SODIUM SELENITE
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DOI:
10.1016/0304-4165(77)90046-0
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发表时间:
1977-01-01
期刊:
影响因子:
--
通讯作者:
HERRMAN, JL
中科院分区:
文献类型:
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作者:
HERRMAN, JL
Properties of a serum selenoprotein which was labeled after the injection of low levels of .**GRAPHIC**. to rats on a Se-adequate diet were investigated. When serum was collected 3 h after injection the label was incorporated preferentially into 1 major serum fraction as shown by polyacrylamide gel electrophoresis. Binding was strong, as demonstrated by the fact that very little label was removed by dialysis against 0.60 M NaCl or 0.50 M .beta.-mercaptoethanol; however, 80% of the 75Se was removed by dialysis against 0.50 M NaOH. MW studies by sodium dodecyl sulfate polyacrylamide gel electrophoresis gave a subunit size of 49,000 under most conditions; when exposed to high concentrations of the detergent (2%) some 75Se was associated with a protein having a MW of 25,000. The native selenoprotein eluted before serum albumin on Sephadex G-150 indicating a MW greater than 67,000. The selenoprotein did not coelute with glutathione peroxidase on DEAE-Sephadex A-50. The prior administration of actinomycin D and cycloheximide resulted in a reduction in incorporation of 75Se into serum by 46 and 70%, respectively, which is consistent with the hypothesis that 75Se is going into newly synthesized protein. The isoelectric point was determined to be 5.4; when heparin was present, the pI was lowered to 3.2. Treatment with 2 M NaCl did not dissociate the protein.cntdot.heparin complex, while exposure to 0.25 M .beta.-mercaptoethanol resulted in the dissociation of 60% of the complex. The fact that Se is so tightly associated with 1 serum protein when administered at levels that would be considered normal under most nutritional conditions suggests an important role for this protein, perhaps in the transport of this essential micronutrient throughout the body.