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Effects of substitutions of amino acids on the thermal stability of the Fv fragments of antibodies
Author(s) -
Yasui Hisashi,
Ito Wataru,
Kurosawa Yoshikazu
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01027-7
Subject(s) - chemistry , circular dichroism , denaturation (fissile materials) , thermal stability , dissociation (chemistry) , chromatography , mass spectrometry , amino acid , monoclonal antibody , stereochemistry , antibody , biochemistry , nuclear chemistry , organic chemistry , biology , immunology
The thermal stability of Fv fragments was examined by circular dichroism (CD) spectrometry and high‐performance liquid chromatography. We analyzed three Fv fragments: that of a monoclonal antibody D1.3 and two derivatives of it. After separation of wild‐type V H and V L fragments, thermal denaturation of each fragment was monitored by CD spectrometry. The results indicated that the dissociation of Fv into V H and V L fragments seemed to be coupled with the denaturation of each fragment and that the thermal denaturation of V H and V L fragments was prevented when they were associated with one another. The analysis of the three Fv fragments also indicated that, in some cases, differences in amino acids even within the CDRs could have significant effects on the thermal stability of the complex between V H and V L fragments.