Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0033687 (proteinuria)
 24,015 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Special methods for the preparation of glycosaminoglycans (GAG) in human dermal tissue and in urine have been developed, enabling in the same preparation the determination of uronic acids as well as the bound organic sulphate without previous use of time-consuming procedures for purification. Special concern has been devoted to the effect of the papain digestion on the recovery of organic sulphate from dermal tissue, and the tissue procedure is further characterized with respect to disintegration, fat extraction and acid hydrolysis. It is shown that human urinary GAG, prepared by the short procedure described, demands a more effective HCL-hydrolysis of organic sulphate than proposed in the literature dealing with purified preparations of GAG. Besides a decrease in the release of sulphate, ineffective hydrolysis may also cause interference in the final sulphate assay, resulting in falsely increased values. It is shown that proteinuria exceeding 0.5 g/l causes a decrease in precipitation yield of GAG and the sulphate/uronic acid ratio. The procedure has resulted in methods of satisfactory accuracy and precision, and due to their large capacity the methods make it possible to get reliable information about the degree of sulphation in dermal and urinary GAG at different conditions in all diseases.
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PMID:Determination of sulphate and uronic acid in glycosaminoglycans of human dermis and in urine. 731 21

Using 3,3'-diclorophenolsulfoftaleinil N-acetyl-beta-D-glucosaminide as a substrate, the apparent activation energy of beta-N-acetylhexosaminidase (Hex) was determined in samples of plasma and urine, as well as in leukocyte and platelet lysates. Incubation with papain produced an increase in this thermodynamic variable for plasma Hex (precursor forms with high molecular mass) that would be caused by the proteolytic action of papain on the Hex A isoenzyme. However, digestion with papain did not significantly modify the activation energy of Hex in leukocyte and platelet lysates (mature enzymatic forms). In 11 healthy subjects and 28 patients with different renal diseases, no statistically significant differences were found with regard to the values obtained in cellular lysates for variations in the activation energy of urinary Hex, regardless of whether they presented normoalbuminuria, microalbuminuria or macroalbuminuria. These results support the hypothesis that even in patients with proteinuria, no significant amounts of plasma Hex precursor forms are found in urine samples, and the source of the enzyme activity is the kidney itself.
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PMID:Effect of partial proteolysis on the activation energy of beta-n-acetylhexosaminidase precursor and mature forms. 1270 38

By means of immunodiffusion and immunoelectrophoresis study has been made of antigenic relationships of Bence Jones proteins, and the three classes of normal and pathological immunoglobulins, 7S gamma, beta(2A), and beta(2M). All thirty-nine Bence Jones proteins studied could be classified into either one of two distinct antigenic types, A or B. Both types are related to the immunoelectrophoretically slow (S) fragment of a papain digest of normal gamma-globulin; B is related more closely than A, but neither has antigenic determinants in common with the fast (F) fragment. The 7S gamma myeloma globulins were either immunological type I or II. The papain digests of these proteins produced the S and F precipitin lines in immunoelectrophoresis but multiple bands in starch gel electrophoresis, especially in the F region. The S fraction of type I myeloma globulins is antigenically similar to Bence Jones protein of type B, and the S component of type II myeloma globulins has antigenic determinants in common with type A Bence Jones protein. Correspondingly, myeloma patients with type I globulins and proteinuria usually excrete type B Bence Jones proteins, whereas patients with type II excrete type A proteins. The F fragment is the part common to normal 7S gamma-globulin and types I and II myeloma globulins but is absent in beta(2A) and beta(2M) pathological globulins and in both types of Bence Jones proteins. Papain digests of beta(2A) myeloma globulins produced a single precipitin line in immunoelectrophoresis. beta(2A) myeloma globulins appeared to have two antigenic units, one in common with type B Bence Jones protein and normal gamma-globulin, and another specific to beta(2A). The beta(2A) myeloma patients excreted type B Bence Jones protein. The papain digest of a macroglobulin produced two precipitin lines, the faster of which had antigenic determinants in common with type B Bence Jones protein, the slower seemed specific for the macroglobulin. Five serum micromolecular globulins proved to be either type A or B Bence Jones proteins. From the above results, an antigenic map was constructed showing which determinants are shared and which are specific for normal 7S gamma-globulin, types I and II myeloma globulins, beta(2A) myeloma globulins, a macroglobulin, and types A and B Bence Jones proteins.
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PMID:Antigenic relationships of Bence Jones proteins, myeloma globulins, and normal human gama-globulin. 1393 73

Whereas intact antibody to rat kidney (7S) produced immediate and sustained proteinuria in rats, univalent fragments (papain digests) of the antibody did not, and divalent fragments (pepsin digests) produced only transitory proteinuria. The antibody fragments differed from the intact antibody in fixing little, if any, complement in vivo which may explain why they did not cause serious renal damage.
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PMID:Antibody to Rat Kidney: In vivo Effects of Univalent and Divalent Fragments. 1779 46