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- W1525535457 abstract "The two disulfide bridges in human pituitary growth hormone were reduced with dithiothreitol in the absence of denaturant. The reduced protein was allowed to autooxidize at pH 8.4, and a reoxidized monomer was obtained in good yield. The reoxidized hormone retained the full biological potency of the native hormone as a growth-promoting and lactogenic agent. Small differences between the native and reoxidized proteins were revealed by viscosity measurements and the rates of tryptic hydrolysis. However, these differences are much smaller than those found between the native hormone and a biologically active reduced tetra-S-carbamidomethylated derivative reported previously. The circular dichroism spectra of the reoxidized and native proteins at pH 8.2 were found to be identical between 205 and 300 mμ. The significance of these findings is discussed in terms of the role of the disulfide bonds in this protein." @default.
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- W1525535457 date "1970-05-01" @default.
- W1525535457 modified "2023-10-12" @default.
- W1525535457 title "Human pituitary growth hormone" @default.
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- W1525535457 doi "https://doi.org/10.1016/0003-9861(70)90315-2" @default.
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