Differential scanning calorimetric studies on bovine serum albumin: II. Effects of neutral salts and urea.


Abstract

Using defatted and SH-blocked bovine serum albumin (BSA), measurements of differential scanning calorimetry (d.s.c.) have been made mainly in NaSCN solution. BSA undergoes a heat-induced conformational transition in a particular range of pH and ionic strength and is separated into two thermally independent units, each of which has different thermostability in acidic and alkaline pH regions. Comparisons were made of the pH dependencies of the enthalpy of thermal denaturation (delta H) and the temperature of thermal denaturation (Td) in 0.01 M NaSCN with those in 0.01 M NaCl. It has been found that the stabilizing effect of NaSCN on BSA is larger than that of NaCl at pH 3.5-8, and that the heat-induced transition occurs by the electrostatic repulsive forces among the positively charged amino acid residues in a segment Arg 184-Arg 216 containing Trp 212 and the primary binding sites of anions. At ionic strength 0.01, the relative effectiveness of anions in suppressing the heat-induced transition and increasing the thermostability of BSA follows the order ClO4- - greater than or equal to SCN- greater than I- greater than SO4(2-) greater than Br- greater than Cl-. At ionic strength 0.1, the heat-induced transition is suppressing in all the salt solutions, and a Td increase follows the order ClO4- greater than or equal to SCN- greater than I- greater than Br- greater than Cl- greater than or equal to SO4(2-). Thus, the highly chaotropic ions thermostabilize BSA more markedly than kosmotropic ions in the low and moderate salt concentrations.(ABSTRACT TRUNCATED AT 250 WORDS) Study holds ProTherm entries: 10815, 10816, 10817 Extra Details: transition 1 thermal denaturation; bovine serum albumin; differential,scanning calorimetry; neutral salts; urea

Submission Details

ID: VhoT3E2j3

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:41 p.m.

Version: 1

Publication Details
Yamasaki M;Yano H;Aoki K,Int. J. Biol. Macromol. (1991) Differential scanning calorimetric studies on bovine serum albumin: II. Effects of neutral salts and urea. PMID:1772822
Additional Information

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P
 

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)


Relevant PDB Entries

Structure ID Release Date Resolution Structure Title
2L7U 2011-05-18 Structure of CEL-PEP-RAGE V domain complex
4LUH 2014-09-17 2.2 Complex of ovine serum albumin with 3,5-diiodosalicylic acid
4LUF 2014-09-17 2.3 Crystal Structure of Ovine Serum Albumin
4F5S 2012-10-03 2.47 Crystal Structure of Bovine Serum Albumin
5ORF 2017-11-15 2.54 Structure of ovine serum albumin in P1 space group
4OR0 2014-06-04 2.58 Crystal Structure of Bovine Serum Albumin in complex with naproxen
4JK4 2013-07-24 2.65 Crystal Structure of Bovine Serum Albumin in complex with 3,5-diiodosalicylic acid
3V03 2012-01-04 2.7 Crystal structure of Bovine Serum Albumin

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
92.4 Serum albumin P14639 ALBU_SHEEP
100.0 Serum albumin P02769 ALBU_BOVIN