Blood-group activity of human Chorionic Gonadotropin
| Autor: | J.F. Mohn, Leopold März, Om P. Bahl |
|---|---|
| Rok vydání: | 1973 |
| Předmět: |
endocrine system
Swine Biophysics Galactosamine Cross Reactions Biology Chorionic Gonadotropin Biochemistry ABO Blood-Group System Human chorionic gonadotropin Serine chemistry.chemical_compound Lewis Blood Group Antigens Lectins Animals Humans Asparagine Saliva Molecular Biology chemistry.chemical_classification Molecular mass Cell Biology Hemagglutination Inhibition Tests Carbohydrate Chromatography Ion Exchange Amino acid Sialic acid chemistry Blood Group Antigens Chromatography Gel Glycoprotein hormones hormone substitutes and hormone antagonists |
| Zdroj: | Biochemical and Biophysical Research Communications. 55:717-723 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/0006-291x(73)91203-5 |
| Popis: | Human Chorionic Gonadotropin has been found to have blood-group A-like activity as shown by the hemagglutination inhibition technique. All of the activity is located in the α subunit of the hormone although it does not contain any N-acetylgalactosamine, a component necessary for the blood-group A activity. Human Chorionic Gonadotropin (hCG) is a glycoprotein hormone comprised of two noncovalently bonded subunits (hCG-α and hCG-β) with approximate molecular weights of 15,000 and 23,000, respectively and each containing about 30% carbohydrate. The monosaccharide and amino acid sequences in both subunits have been recently established (1–4). The carbohydrate moiety of hCG-α is made up of D-galactose, D-mannose, N-acetyl-D-glucosamine and sialic acid while that of hCG-β contains N-acetyl-D-galactosamine and L-fucose, in addition to the above monosaccharides. Furthermore, the carbohydrate part of the hCG-β molecule has some unusual structural features inasmuch as two types of carbohydrate-protein linkages, N-acetylglucosaminyl asparagine and N-acetylgalactosaminyl serine are present in the same molecule. In this respect the hormone resembles mucins on the one hand and the serum glycoproteins on the other. These structural considerations prompted an examination of the molecule for various blood-group activities. This communication presents the results of such an investigation and their possible physiological significance. |
| Databáze: | OpenAIRE |
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