Premium
N‐Terminal Sequence of Pig Brain Choline Acetyltransferase Purified by a Rapid Procedure
Author(s) -
Braun Axel,
Barde YvesAlain,
Lottspeich Friedrich,
Mewes Werner,
Thoenen Hans
Publication year - 1987
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1987.tb13121.x
Subject(s) - choline acetyltransferase , enzyme , chromatography , chemistry , elution , biochemistry , choline , peptide sequence , amino acid , electrophoresis , gel electrophoresis , polyacrylamide gel electrophoresis , antibody , sequence (biology) , affinity chromatography , biology , acetylcholine , gene , immunology , endocrinology
A procedure is reported that allows the purification and amino terminal sequencing of pig brain choline acetyltransferase. The enzyme (present in extremely low amounts in this tissue) is eluted together with its antibody from an affinity column by a mild pH shift and the resulting enzyme‐antibody complex separated by gel electrophoresis. The band corresponding to the enzyme is electroeluted from the gel using volatile solutions allowing the direct determination of the amino acid composition and partial sequence. The first 11 residues are: Pro‐IIe‐Leu‐Glu‐Lys‐Thr‐Pro‐Pro‐Lys‐Met‐Ala.