PMID: 14414439Jan 1, 1960Paper

The binding of myoglobin by plasma protein

The Journal of Experimental Medicine
W LATHEM

Abstract

When added to dog plasma in vitro and in vivo, myoglobin was bound to plasma protein in a concentration which, maximally, averaged 21 +/- 6 mg. per cent. Electrophoretically, bound myoglobin was separated from free myoglobin and migrated between alpha-2 and beta globulin. The electrophoretic characteristics of protein-bound myoglobin were similar to, although not identical with, those of protein-bound hemoglobin. The maximal binding capacity of plasma for myoglobin was less than for hemoglobin, which averaged 123 mg. per cent. At concentrations below the maximal binding capacity, from 15 to 50 per cent of the myoglobin was in the free, unbound state, differing from hemoglobin which was completely bound at all concentrations below the binding capacity. When myoglobin and hemoglobin were added together to plasma, hemoglobin appeared to interfere with the binding of myoglobin or to replace it at the binding sites. Myoglobin, however, did not appear to interfere with the binding of hemoglobin. These observations suggested that myoglobin and hemoglobin were bound at least in part by the same protein. When myoglobin was given intravenously, free myoglobin was excreted in the urine, whereas protein-bound myoglobin was not excreted. Th...Continue Reading

References

Mar 1, 1959·The Journal of Clinical Investigation·W LATHEM, W E WORLEY

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Citations

Jan 1, 1987·Toxicon : Official Journal of the International Society on Toxinology·M M Azevedo-MarquesP Cupo
May 1, 1973·The Journal of Cell Biology·N SimionescuG E Palade
Feb 1, 1967·The American Journal of Medicine·B E FavaraE G Porter
Sep 1, 1960·Archives internationales de physiologie et de biochimie·F GREGOIRE
Apr 15, 1971·Klinische Wochenschrift·H J Braun
Jan 1, 1978·Acta Medica Scandinavica. Supplementum·B SchersténG Jonsson
Jul 1, 1965·The American Journal of Medicine·C F HINZJ LARNER

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