Literature DB >> 22326

The state of aggregation of red deer (Cervus elaphus L.) beta-lactoglobulin preparations near neutral pH.

E I McDougall, J C Stewart.   

Abstract

1. The state of aggregation of four red-deer (Cervus elaphus L.) beta-lactoglobulin preparations and a control ox beta-lactoglobulin A preparation was studied by sedimentation-equilibrium experiments at pH 6.5 and 20 degrees C. 2. Three of the deer preparations and the ox control each behaved as a monomer-dimer system, with a value of log K (where K is the association constant in litres/mol) in the range 5.4-5.5. 3. When one of these deer preparations was examined in the presence of dithiothreitol, log K appeared to decrease to 4.5.4. One deer preparation, comprising recovered material, appeared to have undergone irreversible changes and to behave like a non-equilibrating system containing monomer, dimer and trimer. 5. The sedimentation-equilibrium properties of the deer monomer was studied in 6M-guanidine hydrochloride at pH 7.0; the mol.wt. was 17600, the second virial coefficient was 3.4 x 10(-3) ml - mol - g-2, and the apparent partial specific volume 0.724 ml/g, a value indicating an appreciable decrease in volume on dissociation and denaturation.

Entities:  

Mesh:

Substances:

Year:  1977        PMID: 22326      PMCID: PMC1183620          DOI: 10.1042/bj1670045

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  18 in total

1.  EQUILIBRIUM ULTRACENTRIFUGATION OF DILUTE SOLUTIONS.

Authors:  D A YPHANTIS
Journal:  Biochemistry       Date:  1964-03       Impact factor: 3.162

2.  [Thermodynamic study of the reversible dissociation of beta-lactoglobulin B by pH greater than 5.5].

Authors:  C GEORGES; S GUINAND; J TONNELAT
Journal:  Biochim Biophys Acta       Date:  1962-06-04

3.  The sulfur chemistry of proteins.

Authors:  R CECIL; J R McPHEE
Journal:  Adv Protein Chem       Date:  1959

4.  Reversible association processes of globular proteins. I. Insulin.

Authors:  R F STEINER
Journal:  Arch Biochem Biophys       Date:  1952-08       Impact factor: 4.013

5.  Location of sulfhydryl and disulfide groups in bovine -lactoglobulins and effects of urea.

Authors:  H A McKenzie; G B Ralston; D C Shaw
Journal:  Biochemistry       Date:  1972-11-21       Impact factor: 3.162

6.  Sedimentation equilibrium of protein solutions in concentrated guanidinium chloride. Thermodynamic nonideality and protein heterogeneity.

Authors:  P Munk; D J Cox
Journal:  Biochemistry       Date:  1972-02-29       Impact factor: 3.162

7.  The calculation of partial specific volumes of proteins in guanidine hydrochloride.

Authors:  J C Lee; S N Timasheff
Journal:  Arch Biochem Biophys       Date:  1974-11       Impact factor: 4.013

8.  Partial specific volumes and interactions with solvent components of proteins in guanidine hydrochloride.

Authors:  J C Lee; S N Timasheff
Journal:  Biochemistry       Date:  1974-01-15       Impact factor: 3.162

9.  On the dissociation of bovine -lactoglobulins A, B, and C near pH 7.

Authors:  H A McKenzie; W H Sawyer
Journal:  Aust J Biol Sci       Date:  1972-10

10.  Dissociation of beta-lactoglobulin near neutral pH.

Authors:  J K Zimmerman; G H Barlow; I M Klotz
Journal:  Arch Biochem Biophys       Date:  1970-05       Impact factor: 4.013

View more
  1 in total

1.  Nitrogenase of Klebsiella pneumoniae. Kinetics of the dissociation of oxidized iron protein from molybdenum-iron protein: identification of the rate-limiting step for substrate reduction.

Authors:  R N Thorneley; D J Lowe
Journal:  Biochem J       Date:  1983-11-01       Impact factor: 3.857

  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.