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Membrane perturbing factor in reticulocyte lysate, which is transiently activated by proteases
Author(s) -
Kenjiro Sakaki,
Masao Sakaguchi,
Kazuki Ota,
Katsuyoshi Mihara
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00842-x
Subject(s) - reticulocyte , lysis , proteases , papain , trypsin , protease , membrane , biochemistry , proteinase k , elastase , proteolysis , chemistry , enzyme , biology , messenger rna , gene
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.