半乳糖基转移酶
高尔基体
乳糖
生物化学
化学
限制
α-乳清蛋白
细胞生物学
生物
生物物理学
酶
乳清蛋白
内质网
机械工程
工程类
作者
Nicholas J. Kuhn,David T. Carrick,Colin J. Wilde
标识
DOI:10.3168/jds.s0022-0302(80)82934-1
摘要
Elucidation of the details of lactose synthesis, in particular its dependence upon alpha-lactalbumin and its location within the lumen of the Golgi apparatus, now allows one to ask useful questions pertaining to its regulation. Attention is directed towards galactosyltransferase itself (EC 2.4.1.22), which appears to be rate-limiting in the uridine nucleotide cycle that supports lactose synthesis, and to those factors that may affect its activity. In laboratory animals alpha-lactalbumin appears to be the major agent of regulation during lactogenesis but is not necessarily limiting at other times, whereas the increase in amount of galactosyltransferase seems largely to account for the rising yield of lactose during lactation. Studies with pinched-off Golgi membrane vesicles, together with measurements of intracellular chemical concentrations, suggest that beta-glucose and uridine diphosphategalactose do not saturate lactose synthesis and are, therefore potentially regulatory features of this process. Further aspects of lactose synthesis that may offer points of regulation include calcium ions, generation of protons within the Golgi lumen, and the generally rate-limiting nature of the Golgi membrane.
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