Cloning and sequencing of a cDNA encoding human milk β-casein
| Autor: | Bo Lönnerdal, Olle Hemell, Karin Hjalmarsson, Sven Bergström, Yvonne Andersson, Anna Karin Sundqvist |
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| Jazyk: | angličtina |
| Předmět: |
Signal peptide
Molecular Sequence Data Biophysics Molecular cloning Biology Biochemistry Homology (biology) Sequence comparison Structural Biology Complementary DNA Genetics Humans Amino Acid Sequence Cloning Molecular Molecular Biology Cloning Base Sequence Nucleic acid sequence Caseins Human milk protein Cell Biology DNA Phosphoproteins Molecular biology Open reading frame Angiotensin-converting enzyme inhibitor Nucleic acid Oligonucleotide Probes Nucleotide sequence Calcium-binding site |
| Zdroj: | FEBS Letters. (1):153-156 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(90)81142-B |
| Popis: | A cDNA of 1065 bp encoding the human milk beta-casein was cloned and sequenced using a synthetic oligodeoxyribonucleotide probe and a human mammary gland library. The nucleotide (nt) sequence contained an open reading frame sufficient to encode the entire amino-acid (aa) sequence of a beta-casein precursor protein consisting of 210 aa and a signal peptide of 15 aa. The nt sequence shows 45-62% homology to those of bovine, ovine, rat, and mouse beta-caseins. The highly phosphorylated site, which is responsible for the calcium-binding capacity of beta-casein, the signal peptide, and a sequence encoding for an inhibitor to the angiotensin-converting enzyme seem highly conserved among the beta-caseins with known sequences. |
| Databáze: | OpenAIRE |
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