The Library
A mass spectrometric study of metal binding to osteocalcin
Tools
UNSPECIFIED (2002) A mass spectrometric study of metal binding to osteocalcin. CHEMISTRY & BIOLOGY, 9 (2). pp. 195-202. ISSN 1074-5521.
Research output not available from this repository.
Request-a-Copy directly from author or use local Library Get it For Me service.
Abstract
Electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry was used to investigate Ca2+, Mg2+, and La3+ binding to bovine bone osteocalcin (OCN). OCN was shown to bind 3 mol Call per mol protein. There was also evidence for the presence of four additional metal binding sites. Ca2+ increased the formation of the OCN dimer. Mg2+ bound to OCN to the same extent as Ca2+ but did not induce the dimerization of OCN. La3+ bound to a lesser extent than either Ca2+ or Mg2+ to OCN and, like Mg2+, did not influence dimerization. Each Gla residue of OCN participates in Ca2+ binding, whereas Mg2+ binding may occur preferentially at sites other than Gla residues. This implies that the different natures of Ca2+- and Mg2+-containing OCN complexes influence the tendency of OCN to form a dimer.
Item Type: | Journal Article | ||||
---|---|---|---|---|---|
Subjects: | Q Science > QD Chemistry | ||||
Journal or Publication Title: | CHEMISTRY & BIOLOGY | ||||
Publisher: | CELL PRESS | ||||
ISSN: | 1074-5521 | ||||
Official Date: | February 2002 | ||||
Dates: |
|
||||
Volume: | 9 | ||||
Number: | 2 | ||||
Number of Pages: | 8 | ||||
Page Range: | pp. 195-202 | ||||
Publication Status: | Published |
Data sourced from Thomson Reuters' Web of Knowledge
Request changes or add full text files to a record
Repository staff actions (login required)
View Item |