Binding of [51Cr]ethylenediaminetetraacetate to proteins of human plasma.
Binding of [51Cr]EDTA to human plasma proteins was investigated using chemical and chromatographic techniques of separation of the proteins and protein fractions. Total plasma proteins isolated with ethanol retained 12.95 +/- 0.46% of the initial plasma activity. Proteins separated by other precipitants retained about 16% of the initial radioactivity. Globulins exhibited the highest binding capacity for [51Cr]EDTA and retained about 11.7% of the initial plasma activity following chromatographic separation. This value represents about 70% of the radioactivity bound by the total proteins of the plasma. gamma-Globulins contributed most of the binding attributed to the globulins and retained about 8.7% of the initial [51Cr]EDTA activity. The repeatedly reported underestimation of the renal glomerular filtration rate when estimated as the clearance of [51Cr]EDTA could be adequately accounted for by the extent of binding of this marker to the plasma proteins.
D001798:Blood Proteins / Q000378:metabolism*; D004492:Edetic Acid / Q000378:metabolism*; D005340:Fibrinogen / Q000378:metabolism; D006801:Humans; D011228:Prealbumin / Q000378:metabolism; D012709:Serum Albumin / Q000378:metabolism; D012712:Serum Globulins / Q000378:metabolism; D005719:gamma-Globulins / Q000378:metabolism
D001798:Blood Proteins; D011228:Prealbumin; D012709:Serum Albumin; D012712:Serum Globulins; D005719:gamma-Globulins; D005340:Fibrinogen; D004492:Edetic Acid