Literature DB >> 18101

Further studies of detergent-induced conformational transitions in proteins. Circular dichroism of ovalbumin, bacterial alpha-amylase, papain, and beta-lactoglobulin at various pH values.

Y Y Su, B Jirgensons.   

Abstract

Mesh：

Substances：

Year:  1977        PMID： 18101     DOI： 10.1016/0003-9861(77)90491-x

Source DB:  PubMed          Journal:  Arch Biochem Biophys        ISSN： 0003-9861            Impact factor:   4.013


× No keyword cloud information.
  4 in total

1.  Circular dichroic study of conformational changes in ovalbumin induced by modification of sulfhydryl groups and disulfide reduction.

Authors:  P P Batra; K Sasa; T Ueki; K Takeda
Journal:  J Protein Chem       Date:  1989-10

2.  Effect of various denaturing treatments on the structure and activity of a purified CP1 complex.

Authors:  B Lagoutte; J Duranton
Journal:  Photosynth Res       Date:  1981-09       Impact factor: 3.573

3.  Structural similarity of chymopapain forms as indicated by circular dichroism.

Authors:  S Solis-Mendiola; R Zubillaga-Luna; A Rojo-Dominguez; A Hernandez-Arana
Journal:  Biochem J       Date:  1989-01-01       Impact factor: 3.857

4.  Microenvironment of tryptophan residues in beta-lactoglobulin derivative polypeptide-sodium dodecyl sulfate complexes.

Authors:  T Imamura; K Konishi
Journal:  J Protein Chem       Date:  1992-06
  4 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.