## Abstract α‐fetoprotein from human fetuses and patients with a hepatocelhlar cancer was isolated and characterized. In accordance with earlier reports, the two proteins had similar electrophoretic mobilities and gave a reaction of immunological identity. They had very similar amino acid compositi
Studies of carcino-fetal proteins: Physical and chemical properties of human α-fetoprotein
✍ Scribed by Erkki Ruoslahti; Markku Seppälä
- Publisher
- John Wiley and Sons
- Year
- 1971
- Tongue
- French
- Weight
- 518 KB
- Volume
- 7
- Category
- Article
- ISSN
- 0020-7136
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
To obtain information on the relationship between a carcino‐fetal protein, α‐fetoprotein, fetal proteins from other species and other human serum proteins including the fetoprotein in patients with hepatocellular cancer, α‐fetoprotein was purified and characterized from the serum of human fetuses. The protein is composed of a single polypeptide chain. A molecular weight of 70,000 was obtained by gel electrophoresis in the presence of SDS and by gel filtration. The isoelectric point of α‐fetoprotein was found to be 4.75. It contains 4.3% carbohydrate with 2 moles of sialic acid per mole of protein. The amino acid composition of α‐fetoprotein was determined.
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## Abstract The synthesis of α‐fetoprotein and other fetal plasma proteins was studied by perfusion of isolated human fetal livers with an artificial medium containing leucine‐1‐^14^C. The rates of release by fetal liver of α‐fetoprotein and albumin were analyzed by measuring the changes in their c
The purified Mo-Fe protein and Fe protein of nitrogenase from Azotobacter vinelandii have molecular weights (MW) of about 216000 and 64000, respectively. The Mo-Fe protein is composed of subunits of about 56000 MW, and the Fe protein has 2 equivalent subunits of about 33000 MW. The isoelectric point