Thermodynamic characterization of the partially unfolded state of Ca2+-loaded bovine α-lactalbumin: Evidence that partial unfolding can precede Ca2+ release

Biochemistry

Volumn 35, Issue 51, 1996, Pages 16753-16759

  Vanderheeren, Geertrui ^a   Hanssens, Ignace ^a   Meijberg, Wim ^b   Van Aerschot, Arthur ^c  

^a UNIVERSITY OF LEUVEN   (Belgium)

^b UNIVERSITY OF GRONINGEN   (Netherlands)

^c REGA INSTITUTE FOR MEDICAL RESEARCH   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA LACTALBUMIN; CALCIUM; LYSOZYME;

ARTICLE; CALCIUM TRANSPORT; CATTLE; CONTROLLED STUDY; ENTHALPY; EQUILIBRIUM CONSTANT; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; THERMODYNAMICS;

ANIMALS; BINDING SITES; CALCIUM; CALORIMETRY, DIFFERENTIAL SCANNING; CATTLE; CIRCULAR DICHROISM; HUMANS; HYDROGEN-ION CONCENTRATION; LACTALBUMIN; MURAMIDASE; MUTATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; RECOMBINANT PROTEINS; THERMODYNAMICS;

BOS TAURUS; BOVINAE;

EID: 0030449744     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9608830     Document Type: Article

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