Amino-acid Sequence of Human Placental Lactogen |
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Authors: | LOUIS M SHERWOOD STUART HANDWERGER WILLIAM D McLAURIN MICHAEL LANNER |
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Institution: | 1.Endocrine Unit, Department of Medicine,Beth Israel Hospital and Harvard Medical School,Boston |
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Abstract: | AN earlier report from this laboratory1 described striking homologies in the amino-acid composition of the peptides obtained from trypsin cleavage of human placental lactogen (HPL) and human growth hormone (HGH) and established a firm biochemical basis for the similarities in biological and immunological activity of the two hormones. The intrachain disulphide bonds were placed in similar locations and the carboxyl-terminal amino-acid sequences were shown to be identical except for one out of fourteen residues2. In other studies3,4, the amino-terminal sequence was determined and noted to be homologous for eleven of the first seventeen residues. We now report the complete amino-acid sequence of HPL and a comparison with the revised structure for HGH recently reported4. These two protein hormones are strikingly similar in structure, being identical in 85% of the corresponding positions. Of twenty-eight amino-acid substitutions, twenty-five are favoured changes and all but two of the twenty-five can be explained in terms of a single base change in the triplet codon5. |
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