Characterization of Ca2+-binding sites in the kidney stone inhibitor glycoprotein nephrocalcin using vanadyl ions: Different metal binding properties in strong and weak inhibitor proteins revealed by EPR and ENDOR

Biochemistry

Volumn 35, Issue 47, 1996, Pages 14703-14709

  Mustafi, Devkumar ^a   Nakagawa, Yasushi ^a  

^a UNIVERSITY OF CHICAGO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM BINDING PROTEIN; CALCIUM ION; CALCIUM OXALATE; ISOPROTEIN; VANADYL DERIVATIVE;

ANIMAL TISSUE; ARTICLE; CALCIUM BINDING; CALCIUM OXALATE STONE; CATTLE; ELECTRON SPIN RESONANCE; METAL BINDING; NEPHROLITHIASIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; STOICHIOMETRY;

ANIMALS; BINDING SITES; CALCIUM; CALCIUM OXALATE; CATTLE; CIRCULAR DICHROISM; ELECTRON SPIN RESONANCE SPECTROSCOPY; GLYCOPROTEINS; IONS; KIDNEY CALCULI; METALS; PROTEIN CONFORMATION; VANADATES;

ANIMALIA; BOS TAURUS; BOVINAE;

EID: 0030473268     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi961200j     Document Type: Article

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