Synthesis of a hydrolase for the membrane-form variant surface glycoprotein is repressed during transformation of Trypanosoma brucei.

Abstract:

:A membrane-bound phospholipase C-like hydrolase present in lysates of bloodstream forms of Trypanosoma brucei rapidly converts the membrane form of the variant surface protein to the soluble form and 1,2-dimyristoylglycerol [(1985) M.A.J. Ferguson et al. J. Biol. Chem., 260, 4963-4968]. The hydrolase is inhibited by p-chloromercuribenzenesulfonate. The synthesis of the enzyme is rapidly repressed upon differentiation of bloodstream forms to procyclic cells and the enzyme activity declines to an undetectable level during subsequent growth of procyclic forms.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Bülow R,Overath P

doi

10.1016/0014-5793(85)81223-0

subject

Has Abstract

pub_date

1985-07-22 00:00:00

pages

105-10

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(85)81223-0

journal_volume

187

pub_type

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