Cloning and sequencing of a cDNA encoding human milk beta-casein.
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.
Lönnerdal
B
B
Department of Nutrition, University of California, Davis 95616.
Bergström
S
S
Andersson
Y
Y
Hjalmarsson
K
K
Sundqvist
A K
AK
Hernell
O
O
D000595:Amino Acid Sequence; D001483:Base Sequence; D002364:Caseins / Q000235:genetics*; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D006801:Humans; D008969:Molecular Sequence Data; D015345:Oligonucleotide Probes; D010750:Phosphoproteins / Q000235:genetics
D002364:Caseins; D015345:Oligonucleotide Probes; D010750:Phosphoproteins; D004247:DNA