As a result of the growing awareness of the involvement of the oligosaccharide moieties of glycoproteins and glycolipids in cell surface recognition and binding phenomena, a wide variety of methods have been developed, many quite recently, for preparing glycoconjugates. The chemical methods used for the attachment of sugars and certain hydrophilic polymers (e.g., polyethylene glycol) are discussed, as are the effects of such modifications on various properties of the protein (immune response, thermal stability and resistance to proteolysis, clearance, and specific binding to cell surface receptors). Enzymatic approaches to glycoconjugate preparation are also considered, and several examples are given of the preparation of model glycolipids, useful in studying cell surface phenomena. In a final section, three areas are considered in which rapid advances seem likely to occur: improved methods for the preparation of glycoconjugates; direct modification of cell surface glycoconjugates; and modification for the purpose of studying location and environment of membrane glycoconjugates.

Preparation, properties, and applications of carbohydrate conjugates of proteins and lipids.

The Wiskott-Aldrich syndrome is an immune deficiency disorder with an impairment of both humoral and cellular immune responses. Metabolic turnover studies of IgG, IgA, IgM, and albumin were conducted in seven patients with the Wiskott-Aldrich syndrome using purified radioiodinated proteins. The survival of each of the proteins studied was significantly shortened with a half-time of 7.5 days for IgG (normal 22.9 +/-4 SD), 3.0 days for IgA (normal 5.8 +/-1), 5.0 days for IgM (normal 10.1 +/-2.1), and 8.6 days for albumin (normal 17, range 13-20); the fractional catabolic rates were correspondingly elevated and the distribution of protein among the body compartments was normal. For three of the four proteins. IgG, IgA, and albumin, the steady-state synthetic rates were generally elevated leading to normal or even elevated serum proteins levels. Thus, in the case of IgA, the synthetic rate averaged five times normal while the fractional degradative rate was twice normal. The resulting serum concentration was, therefore, significantly elevated, IgM represented an exception to this pattern in that the increased rate of degradation was not counterbalanced by an increased synthetic rate and, therefore, the serum levels were low. Albumin clearance studies using albumin-(51)Cr showed gastrointestinal protein loss in these patients to be slightly greater than normal, but this could account for only a small fraction of the hypercatabolism observed. There was no proteinuria or abnormalities of thyroid, adrenal, renal, or liver function. Thus, none of the previously recognized causes of increased serum protein catabolism were present. Patients with the Wiskott-Aldrich syndrome, therefore, have a unique disorder of serum protein metabolism characterized by endogenous hypercatabolism of at least four major serum proteins. This phenomenon may be related to reticuloendothelial hyperfunction since the Wiskott-Aldrich syndrome is associated with reticuloendothelial hyperplasia and accelerated clearance of colloidal materials from the plasma.

https://dm5migu4zj3pb.cloudfront.net/manuscripts/106000/106731/JCI71106731.pdf

Hypercatabolism of IgG, IgA, IgM, and albumin in the Wiskott-Aldrich syndrome: A unique disorder of serum protein metabolism

/pdf/measurement-of-intracellular-albumin-in-rat-liver-2xvb2yqqso.pdf

Measurement of intracellular albumin in rat liver

Adult albino rats were injected intravenously with labelled homologous albumin, globulins and fibrinogen. Labelling was done with acid rhodamine B (C.I. No. 45100) and fluorescein isothiocyanate. The amount of fluorescent dye bound to proteins was measured spectrophotometrically. Paper electrophoretic mobility and clotting time of fibrinogen were also checked after labelling. As a control, free fluorescent dye solutions were injected into another lot of rats.Animals were killed at intervals from 10 minutes to 12 days. Blood samples were taken to determine spectrophotometrically the concentration of labelled proteins in the circulation. Paraffin or unfixed fresh frozen sections from all tissues were examined with the fluorescence microscope.Histoimmunological studies were also made using fluorescent antibody against the different rat serum fractions. Coons's technique was applied to tissue sections from normal rats or from animals previously injected with unlabelled serum fractions and killed between 3 and...

Extravascular distribution of fluorescent albumin, globulin and fibrinogen in connective tissue structures:

India ink or other finely divided agents (trypan blue, saccharated iron oxide, thorotrast, polystyrene latex) were injected intravenously into mice, and sheep erythrocyte stroma injected subsequently by the same route.

The splenic uptake of stroma carrying a tag of 131I was consistently higher in mice treated with the `blockading' agents than in untreated controls, the difference in some experiments being greater than ten-fold.

In addition to promoting the splenic uptake of antigen, some of the finely divided agents also enhanced the formation of anti-sheep red cell haemolysin in mice immunized with a single intravenous injection of sheep erythrocyte stroma.

India ink injected intravenously caused a significant rise in the splenic weight of mice.

Stimulation of splenic antigen uptake and of antibody response in mice by India ink or other "blockading" agents.

Distinction between catabolism of native and denatured proteins by the isolated perfused liver after carbon loading.

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Distinction between catabolism of native and denatured proteins by the isolated perfused liver after carbon loading.