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E L HESS

Publications and source records attributed to E L HESS.

27 records · Page 2Linked to original sources
PubMed1953

Fluorescein-conjugated bovine albumin; physical and biological properties.

Fluorescein-bovine albumin conjugates have been prepared and found not to differ appreciably in size, shape, and homogeneity from the precursor, bovine serum albumin. Fluorescein has also been conjugated to rat plasma proteins. Their disappearance rates from the circulation of rats correspond with those obtained from the use of isotope labeling. Their sites of localization in rat tissues were shown to be in the cytoplasm but not in the nuclei of Kupffer cells, fixed macrophages, granulocytes, and proximal renal tubules. Adsorption to endothelium was a characteristic finding. Extracellular localizations were predominantly in the lumina of blood vessels and proximal renal tubules (but never in the lumina of collecting tubules), and the interstitial fluid of skeletal and cardiac muscle (but not that of glandular organs such as the adrenals, liver, and spleen). BAC absorption from the skin of rabbits requires days whereas sodium fluorescein absorption is measured in hours, attesting to the persistence of the colloidal state of BAC in vivo. Fluorescein conjugates have been used to visualize the transcapillary passage of circulating proteins in the mesenteric circulation of frogs and rats by direct microscopic observation and found to diffuse slowly in the manner predicted for plasma proteins. The normal cutaneous vessels of the rat are impermeable in the gross to the labeled proteins; second degree burn promptly increases the permeability of these vessels rendering the presence of the label detectable in the gross in the skin. The process of labeling does not render guinea pig albumin antigenic, although slight antigenicity results from labeling whole plasma protein. It is believed that sufficient biological evidence is presented to support the conclusion that fluorescein-conjugated plasma proteins, particularly albumin, behave in vivo like their native precursors.

Animals↗
PubMed1950

The intrinsic viscosity of mixed protein systems, including studies of plasma and serum.

Experimental evidence is presented that the intrinsic viscosity of solutions of mixed proteins obeys the additive equation See PDF for Equation. The datum serves to characterize the system, and combined with other analytical techniques and fractionation procedures, enables one to analyze and characterize subfractions. The plasmas and sera of clinically "normal" individuals give intrinsic viscosity values agreeing with calculated values. The intrinsic viscosity values for pathological plasmas and sera in all cases are greater than normal and reflect the augmented levels of those proteins fibrinogen, alpha(2)-globulins, and gamma-globulins occurring in the pathological state. The method is readily adaptable to routine clinical use and furnishes a measure of the departure from normal of protein levels in serum and plasma.

Blood↗