BIOCOLLOIDS IN NORMAL HUMAN URINE: II. PHYSICOCHEMICAL AND IMMUNOCHEMICAL CHARACTERISTICS

1958 ◽  
Vol 36 (11) ◽  
pp. 1167-1175 ◽  
Author(s):  
T. Webb ◽  
B. Rose ◽  
A. H. Sehon
Keyword(s):  
Molecular Weight ◽  
Normal Serum ◽  
Low Molecular Weight ◽  
Free Diffusion ◽  
Albumin Fraction ◽  
Serum Component ◽  
Normal Human ◽  
Normal Urine ◽  
Immunochemical Characteristics ◽  
Serum Components

The biocolloids of normal urine were separated by electrophoresis on starch and compared with similarly prepared fractions of serum by ultracentrifugal, free diffusion, and immunochemical techniques. The albumin fraction of urine was indistinguishable from the serum component. The urinary γ2-globulins were shown to consist of low molecular weight (10,000) fragments of the normal serum components. The other globulins of the urine were antigenically related to some of the serum components but appeared to contain lower molecular weight materials. Some of the components of normal serum could not be detected in the urine and the urine contained at least two components which were not present in the serum.

BIOCOLLOIDS IN NORMAL HUMAN URINE: II. PHYSICOCHEMICAL AND IMMUNOCHEMICAL CHARACTERISTICS

1958 ◽  
Vol 36 (1) ◽  
pp. 1167-1175 ◽  
Author(s):  
T. Webb ◽  
B. Rose ◽  
A. H. Sehon
Keyword(s):  
Molecular Weight ◽  
Normal Serum ◽  
Low Molecular Weight ◽  
Free Diffusion ◽  
Albumin Fraction ◽  
Serum Component ◽  
Normal Human ◽  
Normal Urine ◽  
Immunochemical Characteristics ◽  
Serum Components

The biocolloids of normal urine were separated by electrophoresis on starch and compared with similarly prepared fractions of serum by ultracentrifugal, free diffusion, and immunochemical techniques. The albumin fraction of urine was indistinguishable from the serum component. The urinary γ2-globulins were shown to consist of low molecular weight (10,000) fragments of the normal serum components. The other globulins of the urine were antigenically related to some of the serum components but appeared to contain lower molecular weight materials. Some of the components of normal serum could not be detected in the urine and the urine contained at least two components which were not present in the serum.

State of iron(III) in normal human serum: low molecular weight and protein ligands besides transferrin

1970 ◽  
Vol 48 (12) ◽  
pp. 1339-1350 ◽  
Author(s):  
Bibudhendra Sarkar
Keyword(s):  
Molecular Weight ◽  
Human Serum ◽  
Binding Capacity ◽  
Normal Serum ◽  
Normal Human Serum ◽  
Void Volume ◽  
Antibody Concentration ◽  
Low Molecular Weight ◽  
Protein Ligands ◽  
Normal Human

A fraction of Fe(III) in normal human serum is bound to both low molecular weight as well as protein ligands besides transferrin. Citrate was shown to be the major Fe(III)-binding substance in the low molecular weight fraction. Amino acids, sugars, and organic acids, such as ascorbate, pyruvate, and lactate, showed very little or no binding to Fe(III) in normal serum. Iron(III)-binding proteins other than transferrin were shown to be present in normal serum when the native serum with [59Fe(III)] was fractionated by (NH4)2SO4 and Sephadex G-150. The presence of these proteins was observed when trace amounts of Fe(III) were added to the normal serum and when the iron-binding capacity was saturated with Fe(III) to 50% and 100%. These proteins were eluted in the void volume of Sephadex G-150 and none of them corresponded electrophoretically to transferrin. The results of the gel filtration of a mixture of [131I]-transferrin and the proteins eluted in the void volume of Sephadex G-150 were strongly in favor of the Fe(III)-proteins as being neither transferrin aggregates nor transferrin adducts with other proteins. Immunoelectrophoresis of the Sephadex G-150 void volume proteins on agar gel against the antibody to transferrin revealed the absence of transferrin. The presence of at least six proteins in this fraction was shown by immunoelectrophoresis. Positive precipitin reactions were obtained with the antibodies to α2-macroglobulin, γG-globulin, γA-globulin, and γM-globulin. At least two more proteins in this fraction remained unidentified. When the same fraction containing [59Fe(III)] was treated with the whole antisera and the precipitates were counted for radioactivity, a typical antigen-antibody reaction curve was obtained as the antibody concentration was increased. Similar experiments with this fraction and antibodies to α2-macroglobulin, γG-globulin, γA-globulin, and γM-globulin failed to show any significant radioactivity in the precipitate. Since this fraction did not contain any transferrin, it was concluded that there are proteins besides transferrin which can act as ligands for Fe(III) in normal blood plasma.

BIOCOLLOIDS IN NORMAL HUMAN URINE: I. AMOUNT AND ELECTROPHORETIC CHARACTERISTICS

1958 ◽  
Vol 36 (1) ◽  
pp. 1159-1166 ◽  
Author(s):  
T. Webb ◽  
B. Rose ◽  
A. H. Sehon
Keyword(s):  
Human Serum ◽  
Electrophoretic Mobility ◽  
Human Urine ◽  
Filter Paper ◽  
Radioactive Iodine ◽  
Normal Serum ◽  
Γ Globulins ◽  
Normal Human ◽  
Normal Urine ◽  
Serum Components

The biocolloids of normal urine have been isolated and characterized by free electrophoresis and electrophoresis on filter paper. An average of 133 mg of material was recovered from 24-hour aliquots of normal urine. This material was composed of at least seven components as revealed by free electrophoresis at pH 8.6. Five of these components were similar in electrophoretic mobility to the five serum components. A relatively large amount of material was present which behaved like the acid mucoproteins of normal serum. No lipoproteins were detected. Some of the components of the urinary biocolloids were shown to be derived from human serum γ-globulins by labelling the latter with radioactive iodine.

Glycosaminoglycan Fractions in Normal Human Urine

1975 ◽  
Vol 12 (1-6) ◽  
pp. 207-211 ◽  
Author(s):  
C. A. Pennock ◽  
R. G. Charles ◽  
D. Stansbie
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Human Urine ◽  
Cetylpyridinium Chloride ◽  
Low Molecular Weight ◽  
High Molecular Weight Material ◽  
Direct Precipitation ◽  
Normal Human ◽  
Normal Urine

A study has been made of glycosaminoglycans in normal urine to determine which are non-dialysable, which are ultrafilterable, and which are precipitable with cetypyridinium chloride or alcohol. The main fractions present in human urine are: (1) High molecular weight material which is non-dialysable and precipitated by alcohol and by cetylpyridinium chloride. (2) High molecular weight material which is non-dialysable and precipitated by alcohol but not by cetylpyridinium chloride. (3) Low molecular weight material which is ultrafilterable and precipitated by alcohol and by cetylpyridinium chloride. (4) Low molecular weight material which is ultrafilterable and precipitated by alcohol but not by cetylpyridinium chloride. The heavy losses of glycosaminoglycans on dialysis have led us to conclude that this method should not be used to study the excretion of these polymers and that direct precipitation with cetylpyridinium chloride, which can be used to isolate both non-dialysable and ultrafilterable macromolecular fractions relevant to the diagnosis of the mucopolysaccharidoses, is the method of choice.

BIOCOLLOIDS IN NORMAL HUMAN URINE: I. AMOUNT AND ELECTROPHORETIC CHARACTERISTICS

1958 ◽  
Vol 36 (11) ◽  
pp. 1159-1166 ◽  
Author(s):  
T. Webb ◽  
B. Rose ◽  
A. H. Sehon
Keyword(s):  
Human Serum ◽  
Electrophoretic Mobility ◽  
Human Urine ◽  
Filter Paper ◽  
Radioactive Iodine ◽  
Normal Serum ◽  
Γ Globulins ◽  
Normal Human ◽  
Normal Urine ◽  
Serum Components

The biocolloids of normal urine have been isolated and characterized by free electrophoresis and electrophoresis on filter paper. An average of 133 mg of material was recovered from 24-hour aliquots of normal urine. This material was composed of at least seven components as revealed by free electrophoresis at pH 8.6. Five of these components were similar in electrophoretic mobility to the five serum components. A relatively large amount of material was present which behaved like the acid mucoproteins of normal serum. No lipoproteins were detected. Some of the components of the urinary biocolloids were shown to be derived from human serum γ-globulins by labelling the latter with radioactive iodine.

scholarly journals A new case of deficiency of the R binder for cobalamin, with observations on minor cobalamin-binding proteins in serum and saliva

Blood ◽  
1982 ◽  
Vol 59 (1) ◽  
pp. 152-156
Author(s):  
R Carmel
Keyword(s):  
Molecular Weight ◽  
Alcohol Abuse ◽  
Incidental Findings ◽  
Clinical Presentation ◽  
Binding Capacity ◽  
Normal Serum ◽  
Serum Component ◽  
Almost All ◽  
Normal Controls ◽  
Low Serum

A patient presented at the age of 77 yr with a low serum cobalamin level. Subsequent study showed that he had persistently very low R binder (TC I) cobalamin-binding capacity in serum (less than 5 ng/liter versus 213 +/- 171 ng/liter in normal controls), and that almost all of his endogenous serum cobalamin was carried by TC II instead of TC I. His saliva also demonstrated virtually undetectable R binder (binding capacity of 31–38 ng/liter versus 41,690 +/- 23,820 ng/liter for control subjects). Unlike previous cases of R binder deficiency, he seemed to maintain normal serum cobalamin levels while receiving monthly cyanocobalamin injections. This and his normal serum unsaturated binding capacity were due to elevated TC II levels. TC II carried 72%-98% of his endogenous cobalamin, the rest being attached to minor binders. As incidental findings, the patient had a serum component of molecular weight of approximately 70,000 that carried 7%- 8% of his endogenous cobalamin and also had small quantities of TC II demonstrable in his saliva. Both these heretofore unappreciated minor peaks were identifiable because of the lack of R binder. The patient's clinical presentation supports the conclusion that R binder deficiency is a benign disorder. Whether his mild hypersegmentation of neutrophils and neuropathy were related to the R binder deficiency or, more likely, arose from coexisting folate deficiency and alcohol abuse, the overall picture contrasts dramatically with the severe clinical sequelae of TC II deficiency.

Combined proteomic and metabonomic studies in three genetic forms of the renal Fanconi syndrome

2007 ◽  
Vol 293 (2) ◽  
pp. F456-F467 ◽  
Author(s):  
Annalisa Vilasi ◽  
Pedro R. Cutillas ◽  
Anthony D. Maher ◽  
Severine F. M. Zirah ◽  
Giovambattista Capasso ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Fanconi Syndrome ◽  
Low Molecular Weight ◽  
Renal Fanconi Syndrome ◽  
Dent’S Disease ◽  
H Nmr ◽  
Low Molecular Weight Proteinuria ◽  
Dent's Disease ◽  
Underlying Mechanisms ◽  
Normal Urine

The renal Fanconi syndrome is a defect of proximal tubular function causing aminoaciduria and low-molecular-weight proteinuria. Dent's disease and Lowe syndrome are defined X-linked forms of Fanconi syndrome; there is also an autosomal dominant idiopathic form (ADIF), phenotypically similar to Dent's disease though its gene defect is still unknown. To assess whether their respective gene products are ultimately involved in a common reabsorptive pathway for proteins and low-molecular-mass endogenous metabolites, we compared renal Fanconi urinary proteomes and metabonomes with normal (control) urine using mass spectrometry and1H-NMR spectroscopy, respectively. Urine from patients with low-molecular-weight proteinuria secondary to ifosfamide treatment (tubular proteinuria; TP) was also analyzed for comparison. All four of the disorders studied had characteristic proteomic and metabonomic profiles. Uromodulin was the most abundant protein in normal urine, whereas Fanconi urine was dominated by albumin.1H-NMR spectroscopic data showed differences in the metabolic profiles of Fanconi urine vs. normal urine, due mainly to aminoaciduria. There were differences in the urinary metabolite and protein compositions between the three genetic forms of Fanconi syndrome: cluster analysis grouped the Lowe and Dent's urinary proteomes and metabonomes together, whereas ADIF and TP clustered together separately. Our findings demonstrate a distinctive “polypeptide and metabolite fingerprint” that can characterize the renal Fanconi syndrome; they also suggest that more subtle and cause-specific differences may exist between the different forms of Fanconi syndrome that might provide novel insights into the underlying mechanisms and cellular pathways affected.

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