Asparagine-linked carbohydrate chains of inducible rat parotid proline-rich glycoprotein contain terminal beta-linked N-acetylgalactosamine.
Asparagine-linked carbohydrate chains of inducible rat parotid proline-rich glycoprotein contain terminal beta-linked N-acetylgalactosamine.
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诱导型大鼠腮腺富含脯氨酸的糖蛋白的天冬酰胺连接的碳水化合物链含有末端 β 连接的 N-乙酰半乳糖胺。
DOI：
10.1023/a:1018562610375
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发表时间：
1997
影响因子：
3
通讯作者：
Bedi,GS
中科院分区：
文献类型：
--
作者：
Bedi,GS
Rats treated with daily injection of DL-isoproterenol for 10 consecutive days (25 mg kg1 body weight) showed marked induction of a proline-rich glycoprotein (GPRP) of 220 kDa. Proteinase K digestion of GPRP produced a homogeneous glycopeptide with an average chemical composition as follows (residues per mol): Pro4, Glx3, Asx2, Gly1, His1, Thr1, Arg1, GlcNAc5, GalNac1, Man3, Gal2–3, and Fuc1. The structural analysis of the asparagine-linked carbohydrate unit was performed by methylation, periodate oxidation and enzymatic degradation. Methylation studies indicated that the three mannosyl residues were substituted at 1,2-, 1,2,4-, and 1,3,6-positions. Fucose, N-acetylgalactosamine, 1.5 residues of galactose and 0.35 residues of N-acetylglucosamine were terminally located and one galactose residue was 1,4-substituted. Approximately four of the 5 N-acetylglucosamine residues were substituted at 1,4-position and approximately 1 residue of N-acetylglucosamine was substituted at 1,4,6-positions. Periodate oxidation studies and exoglycosidase results were consistent with the methylation data. Based on the results of Smith degradation, methylation and sequential exoglycosidase digestions a triantennary oligosaccharide structure having terminal N-acetylgalactosamine in one of the branches is proposed for the major Asn-linked carbohydrate moiety of GPRP.
