作者: Keiko Murakami , Hiroshi Nagura , Masataka Yoshino
DOI: 10.1016/0003-2697(80)90479-0
关键词: In vitro 、 Enzyme 、 Yeast 、 AMP deaminase 、 Intracellular 、 Saccharomyces cerevisiae 、 Allosteric regulation 、 Biology 、 AMP deaminase activity 、 Biochemistry
摘要: Abstract A permeabilization method which allows the assay of several intracellular enzymes within boundaries yeast cell wall is described. Toluene treatment was found to make cells completely permeable exogenous substrates, and did not leak out treated cells. This also compared with techniques reported previously. Electron microscopic examination toluene-treated indicated that they were essentially intact. The kinetic properties AMP deaminase, examined in permeabilized cells, including allosteric regulation by polyamine Zn2+, suggest some differences protein interactions for deaminase situ vitro.