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神经细胞黏附分子N-CAM的硫酸化和磷酸化

Sulfation and phosphorylation of the neural cell adhesion molecule, N-CAM.

作者信息

Sorkin B C, Hoffman S, Edelman G M, Cunningham B A

出版信息

Science. 1984 Sep 28;225(4669):1476-8. doi: 10.1126/science.6474186.

DOI:10.1126/science.6474186
PMID:6474186
Abstract

Embryonic chicken brain tissue cultured in media containing 35S-labeled sulfate or 32P-labeled phosphate incorporated 35S or 32P into the neural cell adhesion molecule (N-CAM). The 35S label was located in asparagine-linked carbohydrates on both glycopeptides (molecular weights, 170,000 and 140,000) but not in the sialic acid. The 32P label was detected in phosphoamino acids in the carboxyl-terminal third of both polypeptides, but the ratio of phosphoserine to phosphothreonine differed in the two species. The sulfated saccharides and phosphoamino acids may provide additional sites for functional control of N-CAM.

摘要

在含有35S标记硫酸盐或32P标记磷酸盐的培养基中培养的鸡胚脑组织,将35S或32P掺入神经细胞黏附分子(N-CAM)中。35S标记位于两种糖肽(分子量分别为170,000和140,000)上与天冬酰胺连接的碳水化合物中,但不在唾液酸中。在两种多肽羧基末端三分之一的磷酸氨基酸中检测到32P标记,但两种糖肽中磷酸丝氨酸与磷酸苏氨酸的比例不同。硫酸化糖类和磷酸氨基酸可能为N-CAM的功能控制提供额外位点。

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