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Effect of different solvent systems on the aggregation and conformation of S ‐carboxymethyl bovine serum albumin
Author(s) -
Harrap B. S.,
Woods E. F.
Publication year - 1965
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360030601
Subject(s) - chemistry , bovine serum albumin , formamide , formic acid , sodium dodecyl sulfate , solvent , urea , serum albumin , chromatography , organic chemistry , biochemistry
The aggregation properties of S ‐carboxymethyl bovine serum albumin (SCM‐BSA) have been shown to be greatly influenced by the presence of thioglycollide esters in the thioglycollic acid used as a reducing medium. Pure thioglycollic acid gives a product which is aggregated at both pH 7 and 9. Disaggregation may be effected by sodium dodecyl sulfate, by covalently linking groups on to the molecule in order to increase the net negative charge, and solvents such as 8 M urea, 14 M formamide, 11.5 M acetic acid, formic acid, and 2‐chloroethanol. The mechanisms underlying disaggregation in these widely differing solvents are discussed. The results confirm previous findings of a single polypeptide chain in serum albumin. The optical rotatory dispersion of BSA and SCM‐BSA have been compared in a variety of solvents. It has been shown that the disulfide crosslinks in BSA are not the limiting factor to α‐helix formation.