Premium
Isolation and characterisation of A wheat albumin
Author(s) -
Ewart J. A. D.
Publication year - 1969
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740201208
Subject(s) - chemistry , carboxymethyl cellulose , absorbance , tryptophan , histidine , chromatography , tyrosine , phenylalanine , cellulose , molecule , albumin , protease , biochemistry , enzyme , organic chemistry , sodium , amino acid
A major albumin from Cappelle‐Desprez wheat flour has been isolated by carboxymethyl‐cellulose chromatography in a sufficiently pure state for characterisation. The water‐soluble protein is free from phenylalanine and histidine, and this enables the purity to be estimated as > 95 %. It appears to consist of a single chain with a mol. wt. of 26,000. The absorbance coefficient at 280 nm is 1.9 × 10 3 , the high value being due to 8 tryptophan and 8 tyrosine residues per molecule. There are 10 S. S bonds but no sulphydryl groups or sugar residues in the molecule. Sedimentation studies indicate that the molecules tend to aggregate in 0.2 M‐NaCl. No protease or amylase activity was detectable.