## Abstract The interactions between the protein, bovine plasma albumin, and surfactant, sodium dodecyl sulfate, have been studied by ^13^Cβnmr spectroscopy at pH 5.4β6.8 in D~2~O solution. The ^13^C chemical shifts and the ^13^C spinβlattice relaxation time of the individual carbons of the surfact
β¦ LIBER β¦
Conformational changes induced by the interaction of sodium dodecyl sulfate with bovine plasma albumin
β Scribed by Masaru Sogami; Motoji Uyeda; Shigenori Ogura
- Book ID
- 115749506
- Publisher
- Elsevier Science
- Year
- 1973
- Weight
- 510 KB
- Volume
- 310
- Category
- Article
- ISSN
- 0005-2795
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
Interactions between bovine plasma album
β
Yoshio Inoue; Shigeru Sase; Riichiro ChΓ»jΓ΄; Shunji Nagaoka; Masaru Sogami
π
Article
π
1979
π
Wiley (John Wiley & Sons)
π
English
β 564 KB
Conformational changes of Ξ±-lactalbumin
β
Satoshi Hamada; Kunio Takeda
π
Article
π
1993
π
Springer
π
English
β 482 KB
Conformational changes of bovine bone os
β
H. Takita; Y. Kuboki
π
Article
π
1995
π
Springer
π
English
β 779 KB
Conformational changes induced in bovine
β
Graham S. Timmins; Michael J. Davies
π
Article
π
1994
π
Elsevier Science
π
English
β 688 KB
The photodynamic action of haematoporphyrin upon bovine serum albumin, spin-labelled at the cysteine-34 residue, has been shown to: (i) increase its susceptibility to proteolysis by chymotrypsin and trypsin, and (ii) increase its susceptibility to denaturation by urea. This is thought to be the resu
Heat induced aggregation of the sodium d
β
Michael M. Wong; Nancy P. Robertson; Joseph Horwitz
π
Article
π
1978
π
Elsevier Science
π
English
β 837 KB
Assay of Na,K-ATPase in plasma membrane
β
Bliss Forbush III
π
Article
π
1983
π
Elsevier Science
π
English
β 381 KB