Isolation and characterization of a biologically active chromium oligopeptide from bovine liver.
Low-molecular-weight chromium-binding substance (LMWCr), the only known naturally occurring Cr-containing polypeptide from mammals and candidate for the biologically active form of chromium, has been isolated for the first time in yields sufficient for spectroscopic studies capable of providing structural and mechanistic data on a molecular level. The results of paramagnetic 1H NMR, electron paramagnetic resonance, and electronic spectroscopic studies indicate that the four chromic ions per polypeptide are probably arranged in an integer-spin tetranuclear assembly, although an alternate possibility, the presence of two dinuclear assemblies, could not be ruled out. This assembly (or assemblies) is bridged by anionic ligands and supported by carboxylates provided by the polypeptide.
Davis
C M
CM
Department of Chemistry, University of Alabama, Tuscaloosa, Alabama, 35487-0336, USA.
Vincent
J B
JB
D017667:Adipocytes / Q000378:metabolism; D000818:Animals; D002417:Cattle; D002852:Chromatography, Ion Exchange; D017608:Chromium Compounds / Q000302:isolation & purification* / Q000378:metabolism; D007328:Insulin / Q000378:metabolism; D008099:Liver / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D009842:Oligopeptides / Q000302:isolation & purification* / Q000378:metabolism; D051381:Rats
D017608:Chromium Compounds; D007328:Insulin; D009842:Oligopeptides