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- W966483229 abstract "Publisher Summary This chapter discusses that although many litres of human serum or kilograms of human serum of Cohn Fraction IV have been the starting material for isolation of human insulin-like growth factors (hIGF), it is possible to obtain sufficient insulin-like growth factor I (rIGF I) from 1 to 2 litres of rat serum for iodination and standards for radioimmunoassay (RIA) and for characterization with highly sensitive methods. As measured in the human hIGF I/Sm C RIA, normal rat serum is from 2 to 4 times as potent as human serum. Moreover, rIGF I is only about one-third as potent as hIGF in this assay. This suggests that the true level of rIGF I in rat serum is about 600 to 900 ng/ml. Workers have isolated rIGF II—multiplication stimulating activity (MSA)—from conditioned medium of Buffalo rat hepatocytes. A method that led to the isolation and characterization of a peptide very similar in amino acid sequence to hIGF II has also been described in the chapter. The heterogeneity of IGF II related peptides in the conditioned medium is a problem. In addition to the rat IGF II isolated, there are at least six additional peptides that probably represent partially processed precursor molecules." @default.
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- W966483229 date "1985-01-01" @default.
- W966483229 modified "2023-09-27" @default.
- W966483229 title "[59] Isolation of rat somatomedin" @default.
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- W966483229 doi "https://doi.org/10.1016/0076-6879(85)09129-7" @default.
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