期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1973
卷号：70
期号：2
页码：303-305
DOI：10.1073/pnas.70.2.303
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Seasonal variations in the properties of rabbit-liver fructose 1,6-bisphosphatase have now been linked to corresponding changes in the levels of proteolytic activity in the liver extracts. Incubation of native fructose 1,6-bisphosphatase with purified liver lysosomes causes a 3-fold increase in catalytic activity at pH 9.2, with a smaller, and variable, decrease in activity tested at pH 7.5. These changes in catalytic properties are accompanied by the appearance of a smaller subunit, as was previously reported for the enzyme treated with subtilisin. AMP, a negative modulator of fructose bisphosphatase activity, protects against this action of lysosomes. This proteolytic modification of fructose bisphosphatase by lysosomal enzymes may play a role in the modulation of gluconeogenesis.
