Correlations in the Structure and Function of Human Placental Lactogen and Human Growth Hormone. II. The Effects of Disulfide Bond Modification on the Conformation of Human Placental Lactogen1
- 1 September 1972
- journal article
- other
- Published by The Endocrine Society in Endocrinology
- Vol. 91 (3) , 728-737
- https://doi.org/10.1210/endo-91-3-728
Abstract
The molecular properties of reduced carboxymethylated, reduced carbamidomethylated and oxidized human placental lactogen have been studied by UV absorption, fluorescence and circular dichroism. Reduction and alkylation of the two disulfide bonds in the presence of urea results in the loss of numerous noncovalent interactions of the native structure and the acquisition of new noncovalent interactions. Oxidized placental lactogen shows an even greater loss in native structure without the formation of new intramolecular bonds. Since lactogenic activity is completely retained in these modified forms of lactogen, it appears that its native three—dimensional structure is not necessary for lactogenic activity. It seems possible, therefore, that a fragment of the polypeptide chain may be sufficient to produce hormonal effects. (Endocrinology91: 728, 1972)Keywords
This publication has 0 references indexed in Scilit: