Leghaemoglobin from Trifolium subterraneum. Purification and characterization.
Leghaemoglobin from the subclover, Trifolium subterraneum cultivar Woogenellup, has been fractionated into at least four electrophoretically distinct components using the ion-exchange chromatographic procedure described by Appleby et al. (Appebly, C.A., Nicola, N.A., Hurrell, J.G.R. and Leach, S.J. (1975) Biochemistry 14, 4444--4450) for soybean leghaemoglobins. Unlike those of soybean, the subclover leghaemoglobins showed no evidence of autoxidation under identical isolation procedures, implying that these proteins have an unusually stable ferrous oxidation state. Circular dichroism in the far-ultraviolet (200--240 nm) indicated a high helicity (approx. 70%) as has been reported for other species of leghaemoglobins. However, circular dichroism in the near-ultraviolet region (240--300 nm) indicated that the haem-protein interactions may be considerably different in the subclover leghaemoglobins and this may explain their atypical resistance to autoxidation and the absence of nicotinate binding in these proteins.
D001665:Binding Sites; D002942:Circular Dichroism; D006420:Hemeproteins / Q000302:isolation & purification*; D007874:Leghemoglobin / Q000302:isolation & purification* / Q000378:metabolism; D009539:Nicotinic Acids / Q000378:metabolism; D010084:Oxidation-Reduction; D010940:Plant Proteins / Q000302:isolation & purification* / Q000378:metabolism; D010944:Plants / Q000032:analysis*; D011485:Protein Binding; D013025:Glycine max / Q000032:analysis; D013053:Spectrophotometry
D006420:Hemeproteins; D007874:Leghemoglobin; D009539:Nicotinic Acids; D010940:Plant Proteins