muramidase and maleic-acid

The adsorption of human serum albumin (HSA) and lysozyme (LSZ) on pure as well as maleic acid (MA) copolymer coated spherical soda lime glass particles was investigated under flowing conditions. Coating the glass particles with two different maleic acid copolymers alters the properties of the particle surface concerning its charge and hydrophobicity in a well-defined gradation. Frontal chromatography was used to determine the surface concentration of the adsorbed proteins and to establish adsorption isotherms. The introduced methodology was demonstrated to provide a powerful means to study protein adsorption at solid/liquid interfaces. Investigations with virginal and protein-preadsorbed glass particles revealed that even under streaming conditions HSA is irreversibly adsorbed, whereas LSZ partially desorbs. For LSZ and HSA the adsorbed amounts and the isotherms strongly depend on the surface "history", i.e. the presence or absence of preadsorbed protein layers, and the kind of surface modification of the glass. Compared to the soda lime glass surface the adsorption of HSA was strongly increased on surfaces modified with a hydrophobic maleic acid copolymer indicating a strong hydrophobic protein-surface interaction. By coating the surface with a hydrophilic and more negatively charged maleic acid copolymer the adsorption of HSA to that surface was lower and comparable to the adsorption onto plain glass due to the electrostatic repulsion between HSA and the modified surface. In contrast the affinity to any of the investigated particle surfaces was generally higher for LSZ than for HSA which can be mainly attributed to the electrostatic attraction between LZS and the surface. The adsorbed amount of LSZ on the copolymer coated particle surfaces was much higher than on the pure soda lime glass particles indicating superposed hydrophobic interactions in the case of the hydrophobic MA copolymer layer and an increased density of anionic sites as well as interactions of LSZ within the three-dimensional (swollen), hydrophilic MA copolymer layer.

Topics: Adsorption; Chromatography; Glass; Humans; Hydrophobic and Hydrophilic Interactions; Maleates; Molecular Weight; Muramidase; Particle Size; Polymers; Protein Binding; Protein Conformation; Proteins; Serum Albumin; Solutions; Static Electricity; Surface Properties

Competitive inhibition of renal tubular transport occurs between low- and high-molecular-weight proteins following intravenous infusion, but this relationship is less clear following de novo glomerular or renal tubular injury. The present study evaluated renal lysozyme and albumin handling following renal tubular injury induced by both low- and high-dose mercuric chloride (0.5 and 2.0 mg/kg) and maleic acid (50 and 400 mg/kg), and following glomerular injury induced by puromycin aminonucleoside (5 mg/100 g) or Adriamycin (5 mg/kg). Subtle renal tubular injury induced only mild isolated albuminuria, while severe tubular injury caused dramatic lysozymuria and moderate albuminuria. However, increased filtration of albumin in these models of glomerular injury did not inhibit lysozyme transport.

Topics: Albumins; Albuminuria; Animals; Biological Transport, Active; Doxorubicin; Kidney Glomerulus; Kidney Tubules; Male; Maleates; Mercuric Chloride; Muramidase; Proteins; Puromycin Aminonucleoside; Rats; Rats, Inbred Strains

During the acute renal tubular dysfunction of Fanconi syndrome and type 2 renal tubular acidosis (FS/RTA2) induced by maleic acid in the unanesthetized dog, we observed: 30 minutes after the onset of FS/RTA2, the urinary excretion of lysosomal enzymes, N-acetyl-beta-glucosaminidase (NAG), beta-glucuronidase (beta-gluc) and beta-galactosidase (beta-galac), increased simultaneously with the anticipated increase in renal clearance of lysozyme; the severities of all these hyperenzymurias increased rapidly, progressively, and in parallel, all reaching a peak some 60 to 80 minutes after their onset; thereafter, while the FS/RTA2 continued undiminished in severity, the severity of the hyperenzymurias decreased rapidly, greatly, progressively, and in parallel; and sodium phosphate loading strikingly attenuated the FS/RTA2 and the hyperenzymurias. Thus, the maleic acid-induced FS/RTA2 is attended by an acute reversible-complex derangement in the renal tubular processing of proteins that: affects not only lysozyme which is normally filtered, but also NAG and other lysosomal enzymes, which are not; and is to some extent functionally separable from that of FS/RTA2. The findings suggest that the derangements in renal processing of lysozyme and lysosomal enzymes are linked, and that a phosphate-dependent metabolic abnormality in the proximal tubule can participate in the pathogenesis of both these derangements and the FS/RTA2.

Topics: Acetylglucosaminidase; Acidosis, Renal Tubular; Animals; beta-Galactosidase; Dogs; Fanconi Syndrome; Female; Galactosidases; Glucuronidase; Hexosaminidases; Injections, Intravenous; Kidney Diseases; Kidney Function Tests; Maleates; Metabolic Clearance Rate; Muramidase; Phosphates