α-D-甘露糖苷酶在人-仓鼠体细胞杂种中的表达。

Expression of alpha-D-mannosidase in man-hamster somatic cell hybrids.

作者信息

Ingram P H, Bruns G A, Regina V M, Eisenman R E, Gerald P S

出版信息

Biochem Genet. 1977 Jun;15(5-6):455-76. doi: 10.1007/BF00520191.

DOI:10.1007/BF00520191

Abstract

Two types of alpha-D-mannosidase isozymes are present in human white blood cells, human diploid fibroblasts, and HeLa cells. One of these (the S isozyme) constitutes the major alpha-D-mannosidase of the human cells, has a pH optimum of 4.4, and is associated with lysosomes. The other (the F isozyme) is most active at pH 6, is acid labile, and is located in the soluble portion of the cytoplasm. The expression of human lysosomal alpha-D-mannosidase was examined in man-hamster hybrid clones, and was found to be concordant with that of phosphohexose isomerase in 54 of 55 primary clones. A locus specifying human lysosomal alpha-D-mannosidase has therfore been assigned to chromosome 19.

摘要

在人类白细胞、人二倍体成纤维细胞和海拉细胞中存在两种α-D-甘露糖苷酶同工酶。其中一种（S同工酶）是人类细胞中的主要α-D-甘露糖苷酶，最适pH为4.4，与溶酶体相关。另一种（F同工酶）在pH 6时活性最高，对酸不稳定，位于细胞质的可溶性部分。在人-仓鼠杂交克隆中检测了人类溶酶体α-D-甘露糖苷酶的表达，发现在55个初级克隆中的54个中，其与磷酸己糖异构酶的表达一致。因此，已将一个指定人类溶酶体α-D-甘露糖苷酶的基因座定位到19号染色体。