title: Membrane perturbing factor in reticulocyte lysate, which is transiently activated by proteases.
abstract: Proteases have been used to examine the topology of proteins on various membranes. We reexamined the conditions of protease treatment for rough microsomal membranes and found that proteinase K degraded the lumenal proteins in the presence of reticulocyte lysate. The lysate treated with either heat or N-ethylmaleimide no longer promoted the degradation. The reticulocyte dependent degradation was also observed with papain, trypsin, and elastase. This activity was transiently generated by treating reticulocyte lysate short-term with trypsin. We thus concluded that a membrane perturbing factor(s) must exist in reticulocyte which is transiently activated by protease treatment.
authors.affiliation: Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Sakaki
authors.forename: M
authors.initials: M
authors.lastname: Sakaguchi
authors.forename: K
authors.initials: K
authors.lastname: Ota
authors.forename: K
authors.initials: K
authors.lastname: Mihara
mesh_terms: D000818:Animals; D004285:Dogs; D019286:Endopeptidase K / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D008861:Microsomes / Q000378:metabolism*; D011817:Rabbits; D012156:Reticulocytes / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D008565:Membrane Proteins; D019286:Endopeptidase K