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：3
页码：661-664
DOI：10.1073/pnas.70.3.661
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Removal of the NH2-terminal region of fructose 1,6-bisphosphatase from rabbit liver by digestion with subtilisin, or changes in conformation in this region of the protein produced by exposure to low concentrations of urea, result in similar changes in catalytic and allosteric properties of the enzyme. These changes include shift of the pH optimum to more alkaline pH, and loss of sensitivity to inhibition by AMP. The conformation changes are monitored by changes in the fluorescence of the single tryptophan residue, which is located near the NH2-terminus. Thus, the tryptophan-containing peptide appears to determine the functional properties of the native enzyme.
