Thurin J, Blaszczyk-Thurin M
Wistar Institute of Anatomy and Biology, Philadelphia, Pennsylvania 19104-4268, USA.
J Biol Chem. 1995 Nov 3;270(44):26577-80. doi: 10.1074/jbc.270.44.26577.
Partial amino acid sequence of GDP-L-fucose:beta-D-galactoside alpha-2-L-fucosyltransferase purified from porcine submaxillary glands was determined. Amino acid sequence analysis yielded 100, 93.3, and 84.2%, and 75, 46.6, and 84.2% sequence identity between 12-, 15-, and 19- amino acid tryptic peptides generated from porcine enzyme and amino acid residues 61-72, 111-125, and 308-326 and 89-100, 139-153, and 338-356 of the human Secretor and H type alpha-2-fucosyltransferases, respectively. Higher amino acid sequence homology of the porcine enzyme with the predicted sequence for the human Secretor locus as compared with H gene-encoded blood group beta-D-galactoside alpha-2-L-fucosyltransferase suggests that porcine alpha-2-fucosyltransferase highly corresponds to the human Secretor gene-encoded enzyme.
测定了从猪颌下腺纯化的GDP-L-岩藻糖:β-D-半乳糖苷α-2-L-岩藻糖基转移酶的部分氨基酸序列。氨基酸序列分析表明,从猪酶产生的12、15和19个氨基酸的胰蛋白酶肽与人类分泌型和H型α-2-岩藻糖基转移酶的氨基酸残基61-72、111-125和308-326以及89-100、139-153和338-356之间的序列同一性分别为100%、93.3%和84.2%,以及75%、46.6%和84.2%。与H基因编码的血型β-D-半乳糖苷α-2-L-岩藻糖基转移酶相比,猪酶与人类分泌型基因座预测序列的氨基酸序列同源性更高,这表明猪α-2-岩藻糖基转移酶与人类分泌型基因编码的酶高度对应。