Functional approach to the catalytic site of the sarcoplasmic reticulum Ca 2+-ATPase: Binding and hydrolysis of ATP in the absence of Ca 2+

Journal of Bioenergetics and Biomembranes

Volumn 36, Issue 3, 2004, Pages 265-273

  Lax, Antonio ^a   Soler, Fernando ^a   Fernández Belda, Francisco ^a  

^a UNIVERSITY OF MURCIA   (Spain)

Author keywords

Ca 2+ ATPase mechanism; Ca 2+ independent ATPase activity; muscle relaxation; rabbit skeletal muscle; sarcoplasmic reticulum Ca 2+ ATPase

Indexed keywords

4 NITROPHENYL PHOSPHATE; ADENOSINE TRIPHOSPHATASE (CALCIUM); ADENOSINE TRIPHOSPHATE; CALCIUM ION; MAGNESIUM ION; VANADIC ACID;

ANIMAL TISSUE; ARTICLE; BINDING AFFINITY; CATALYSIS; CONTROLLED STUDY; CYTOPLASM; FEMALE; HYDROLYSIS; NONHUMAN; PH; RABBIT; SARCOPLASMIC RETICULUM;

ADENOSINE TRIPHOSPHATE; ANIMALS; CALCIUM-TRANSPORTING ATPASES; CATALYSIS; FEMALE; HYDROLYSIS; MAGNESIUM; MODELS, MOLECULAR; MUSCLE, SKELETAL; PHOSPHORUS RADIOISOTOPES; PROTEIN BINDING; RABBITS; SARCOPLASMIC RETICULUM; VANADATES;

ANIMALIA; ORYCTOLAGUS CUNICULUS;

EID: 3042855278     PISSN: 0145479X     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:JOBB.0000031978.15139.49     Document Type: Article

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