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Cloning and sequencing of a cDNA encoding human milk β‐casein
Author(s) -
Lönnerdal Bo,
Bergström Sven,
Andersson Yvonne,
Hjalmarsson Karin,
Sundqvist Anna Karin,
Hemell Olle
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81142-b
Subject(s) - complementary dna , peptide sequence , signal peptide , microbiology and biotechnology , biology , nucleic acid sequence , casein , biochemistry , cdna library , open reading frame , amino acid , cloning (programming) , homology (biology) , peptide , dna , gene , computer science , programming language
A cDNA of 1065 bp encoding the human milk β‐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 β‐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 β‐caseins. The highly phosphorylated site, which is responsible for the calcium‐binding capacity of β‐casein, the signal peptide, and a sequence encoding for an inhibitor to the angiotensin‐converting enzyme seem highly conserved among the β‐caseins with known sequences.