Premium
Release and purification of trypanosoma brucei variant surface glycoprotein
Author(s) -
Cross George A. M.
Publication year - 1984
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240240107
Subject(s) - trypanosoma brucei , iodoacetamide , glycoprotein , pmsf , lysis , biochemistry , reagent , chemistry , cleavage (geology) , biology , enzyme , organic chemistry , paleontology , cysteine , fracture (geology) , gene
Conditions affecting the solubilization of variant surface glycoprotein (VSG) from Trypanosoma brucei have been investigated. The results obtained form the basis for a convenient and efficient method for VSG purification. VSG release from the cell surface was temperature‐dependent, following osmotic lysis at 0 °C, and was inhibited by low concentrations of Zn 2+ but not by tosyl‐lysine chloromethyl‐ketone (TLCK), phenylmethylsulfonylfluoride (PMSF), or iodoacetamide. These and other results eliminated the possibility that release was due to proteolytic cleavage of the C‐terminal hydrophobic tail present on newly synthesized VSG. Bolton and Hunter reagent reacted with several components on living cells.