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- W2000957175 abstract "Abstract 1. 1. Albumin purified from rhesus monkey (MSA) shows immunological cross-reactivity with human serum albumin (HSA) by RIA. 2. 2. The amino-terminal sequence of MSA shows a high degree of homology to HSA. 3. 3. Thirty minutes after injection of radioactive leucine directly into the portal vein, albumin was purified chemically from the liver, kidneys and serum. 4. 4. At this time, 15% of the label was incorporated into liver homogenate protein. 5. 5. A highly labelled immunoreactive albumin form was purified from liver to constant specific radioactivity and separated from tissue and serum albumin. 6. 6. The specific radioactivity of this proalbumin was 36-times higher than the specific radioactivity of albumin in liver tissue. 7. 7. These similarities to HSA suggest that this non human primate species can serve as a useful model of human albumin synthesis in vivo ." @default.
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- W2000957175 date "1980-01-01" @default.
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- W2000957175 title "Purification and characterization of monkey albumin and proalbumin" @default.
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- W2000957175 doi "https://doi.org/10.1016/0305-0491(80)90278-3" @default.
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