Hemoglobin dendrimers: functional protein clusters.
A cluster of cross-linked hemoglobin tetramers was prepared by conjugating active esters to amino groups of a starburst dendrimer. Comparison of oxygen-binding properties of the protein cluster to those of nonclustered species reveals an increase in affinity and a decrease in cooperativity in the cluster. The altered oxygen-binding properties are assigned to protein-protein interactions.
Kluger
Ronald
R
Davenport Chemical Research Building, Department of Chemistry, University of Toronto, Ontario, Canada M5S 3H6. rkluger@chem.utoronto.ca
Zhang
Jie
J
D000328:Adult; D002851:Chromatography, High Pressure Liquid; D003432:Cross-Linking Reagents / Q000737:chemistry*; D019281:Dimerization; D004591:Electrophoresis, Polyacrylamide Gel; D006454:Hemoglobins / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D008970:Molecular Weight; D010100:Oxygen / Q000737:chemistry / Q000378:metabolism; D012459:Salicylates / Q000737:chemistry*; D013056:Spectrophotometry, Ultraviolet
D003432:Cross-Linking Reagents; D006454:Hemoglobins; D012459:Salicylates; C475202:trimesoyl tris(dibromosalicylate); D010100:Oxygen