CLONING AND SEQUENCING OF A CDNA-ENCODING HUMAN-MILK BETA-CASEIN

被引：22

作者：

LONNERDAL, B

BERGSTROM, S

ANDERSSON, Y

HJALMARSSON, K

SUNDQVIST, AK

HERNELL, O

机构：

[1] UMEA UNIV, DEPT BIOCHEM, S-90187 UMEA, SWEDEN

[2] UMEA UNIV, DEPT PEDIAT, S-90187 UMEA, SWEDEN

[3] SYMBICON AB, UMEA, SWEDEN

[4] UNIV CALIF DAVIS, DEPT NUTR, DAVIS, CA 95616 USA

来源：

FEBS LETTERS | 1990年 / 269卷 / 01期

关键词：

Angiotensin-converting enzyme inhibitor; Calcium-binding site; Human milk protein; Nucleotide sequence; Sequence comparison;

D O I：

10.1016/0014-5793(90)81142-B

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. © 1990.

引用

页码：153 / 156

页数：4

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[1] PILIATION CONTROL MECHANISMS IN NEISSERIA-GONORRHOEAE [J].