000 01651 a2200469 4500
005 20250513090254.0
264 0 _c19960603
008 199606s 0 0 eng d
022 _a0264-6021
024 7 _a10.1042/bj3140943
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aThumser, A E
245 0 0 _aMutations of recombinant rat liver fatty acid-binding protein at residues 102 and 122 alter its structural integrity and affinity for physiological ligands.
_h[electronic resource]
260 _bThe Biochemical journal
_cMar 1996
300 _a943-9 p.
_bdigital
500 _aPublication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
650 0 4 _aAmino Acid Sequence
650 0 4 _aAnimals
650 0 4 _aCarrier Proteins
_xchemistry
650 0 4 _aCircular Dichroism
650 0 4 _aDansyl Compounds
650 0 4 _aFatty Acid-Binding Protein 7
650 0 4 _aFatty Acid-Binding Proteins
650 0 4 _aFatty Acids
_xmetabolism
650 0 4 _aFluorescent Dyes
650 0 4 _aLigands
650 0 4 _aLiver
_xmetabolism
650 0 4 _aMutagenesis, Site-Directed
650 0 4 _aMyelin P2 Protein
_xchemistry
650 0 4 _aNeoplasm Proteins
650 0 4 _aNerve Tissue Proteins
650 0 4 _aPoint Mutation
650 0 4 _aProtein Conformation
650 0 4 _aRats
650 0 4 _aRecombinant Proteins
_xchemistry
650 0 4 _aSpectrometry, Fluorescence
650 0 4 _aSubstrate Specificity
700 1 _aVoysey, J
700 1 _aWilton, D C
773 0 _tThe Biochemical journal
_gvol. 314 ( Pt 3)
_gp. 943-9
856 4 0 _uhttps://doi.org/10.1042/bj3140943
_zAvailable from publisher's website
999 _c8614838
_d8614838