Literature DB >> 873903

Antibody as immunological probe for studying refolding of bovine serum albumin. Refolding within each domain.

J M Teale, D C Benjamin.   

Abstract

Antiserum to bovine serum albumin was fractionated into populations of antibody directed against party, an apparent pathway of refolding within each domain was obtained which is consistent with the proposed evolutionary pathway of the albumin molecule. The COOH-terminal one-third of each domain refolds faster than the NH2-terminal two-thirds of each respective domain. In addition, further evidence in given for a correlation between the rate of refolding and the degree of interdomain influence that might restrict refolding.

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Year:  1977        PMID: 873903

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  5 in total

1.  Antibody-detected folding: kinetics of surface epitope formation are distinct from other folding phases.

Authors:  C S Raman; R Jemmerson; B T Nall
Journal:  Protein Sci       Date:  2000-01       Impact factor: 6.725

2.  Peptide antisera as sequence-specific probes of protein conformational transitions: calmodulin exhibits calcium-dependent changes in antigenicity.

Authors:  J Gariépy; T A Mietzner; G K Schoolnik
Journal:  Proc Natl Acad Sci U S A       Date:  1986-12       Impact factor: 11.205

3.  Conformational change of bovine serum albumin by heat treatment.

Authors:  K Takeda; A Wada; K Yamamoto; Y Moriyama; K Aoki
Journal:  J Protein Chem       Date:  1989-10

4.  Secondary structural changes of large and small fragments of bovine serum albumin in thermal denaturation and in sodium dodecyl sulfate denaturation.

Authors:  K Takeda; S Hamada; A Wada
Journal:  J Protein Chem       Date:  1993-04

5.  Folding of firefly luciferase during translation in a cell-free system.

Authors:  V A Kolb; E V Makeyev; A S Spirin
Journal:  EMBO J       Date:  1994-08-01       Impact factor: 11.598

  5 in total

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