Thermal stability and aggregation of creatine kinase from rabbit skeletal muscle. Effect of 2-hydroxypropyl-β-cyclodextrin

Biophysical Chemistry

Volumn 148, Issue 1-3, 2010, Pages 121-130

  Maloletkina, Olga I ^a   Markossian, Kira A ^a   Belousova, Lyubov V ^b   Kleimenov, Sergey Yu ^a   Orlov, Victor N ^b   Makeeva, Valentina F ^a   Kurganov, Boris I ^a  

^a BACH INSTITUTE OF BIOCHEMISTRY   (Russian Federation)

^b MOSCOW STATE UNIVERSITY   (Russian Federation)

Author keywords

2 Hydroxypropyl cyclodextrin; Aggregation; Creatine kinase; Denaturation; Inactivation

Indexed keywords

2 HYDROXYPROPYL BETA CYCLODEXTRIN; CREATINE KINASE;

ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DIFFERENTIAL SCANNING CALORIMETRY; ENZYME ACTIVATION; ENZYME ANALYSIS; ENZYME DENATURATION; ENZYME INACTIVATION; ENZYME STABILITY; HYDRODYNAMICS; LIGHT SCATTERING; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; QUANTITATIVE ANALYSIS; RABBIT; SKELETAL MUSCLE; THERMOSTABILITY;

ANIMALS; BETA-CYCLODEXTRINS; CREATINE KINASE; ENZYME ACTIVATION; ENZYME STABILITY; KINETICS; LIGHT; MUSCLE, SKELETAL; PARTICLE SIZE; PROTEIN BINDING; PROTEIN DENATURATION; RABBITS; SCATTERING, RADIATION; SPECTROMETRY, FLUORESCENCE; TEMPERATURE;

ORYCTOLAGUS CUNICULUS;

EID: 77951977567     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2010.03.005     Document Type: Article

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