SIMILARITY OF THE NUCLEOTIDE-SEQUENCES OF RAT ALPHA-LACTALBUMIN AND CHICKEN LYSOZYME GENES
SIMILARITY OF THE NUCLEOTIDE-SEQUENCES OF RAT ALPHA-LACTALBUMIN AND CHICKEN LYSOZYME GENES
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DOI:
10.1038/308377a0
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发表时间:
1984-01-01
期刊:
影响因子:
64.8
通讯作者:
SAFAYA, SK
中科院分区:
文献类型:
--
作者:
QASBA, PK;SAFAYA, SK
α-Lactalbumin (α-LA) is a milk protein that interacts with the enzyme galactosyltransferase, modifying its substrate specificity in a way which promotes the transfer of galactose to glucose, resulting in aβ–1→4 glycosidic linkage and the synthesis of lactose1,2. Lysozyme, an enzyme which catalyses the hydrolysis of aβ–1→4 glycosidic linkage in polysaccharides, has been shown to be structurally related toα-LA and it has been proposed that they have arisen from a common ancestral gene3. To compare their evolutionary relationships, we report here the complete nucleotide sequence of the ratα-LA gene, including its 5′-flanking sequences, and compare its gene structure with the chicken egg-white lysozyme gene4. Both genes contain three introns at similar positions. The first three exons of the two genes have similar nucleotide sequences. The fourth exon ofα-LA, which partly codes for the C-terminal residues of the protein, essential for its interaction with galactosyltransferase5,6, is markedly different from the corresponding exon of the lysozyme gene and is preceded by two (TG)nrepeats.