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.

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.

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.

The Binding of Lithium Carmine to a2-Macroglobulin

1969 ◽  
Vol 24 (11) ◽  
pp. 1442-1447 ◽  
Author(s):  
J. J. Picard ◽  
J. F. Heremans
Keyword(s):  
Human Serum ◽  
Density Gradient ◽  
Protein Complex ◽  
Gel Filtration ◽  
Heavy Fraction ◽  
Normal Human Serum ◽  
Density Gradient Ultracentrifugation ◽  
Γ Globulins ◽  
Normal Human

The colloidal dye lithium carmine was added in vitro to normal human serum. Electrophoretic experiments showed that the dye was associated mainly with α2-globulins, small amounts with the albumin and only traces with the γ-globulins. The main complex was eluted with the macroglobulin peak obtained by gel filtration on Sephadex G-200 and sedimented in the heavy fraction on density gradient ultracentrifugation. The dye-protein complex could be precipitated with an antiserum specific for a2-macroglobulin. Gel filtration of a solution of pure a2-macroglobulin, to which lithium carmine was added, demonstrated that the dye was bound to this protein.

scholarly journals A Hypertransfused Mouse Assay for Thrombopoietic Factors

Blood ◽  
1973 ◽  
Vol 42 (3) ◽  
pp. 423-428 ◽  
Author(s):  
George W. Cooper ◽  
Barbara Cooper ◽  
A. Lawrence Ossias ◽  
Esmail D. Zanjani
Keyword(s):  
Human Serum ◽  
Whole Blood ◽  
Hodgkin's Disease ◽  
Healthy Donor ◽  
Hodgkin’S Disease ◽  
Normal Serum ◽  
Normal Platelet ◽  
Quantitative Separation ◽  
Thrombocytopenic Patient ◽  
Normal Human

Abstract A method was developed for the quantitative separation of platelets from CF1 mouse whole blood. This made it possible to determine the platelet incorporation of 35S-sulfate without the necessity of doing platelet counts. Daily hypertransfusions of the mice to three to four times normal platelet levels for 4-5 days significantly reduced platelet uptake of radiosulfate to an average of about 40% of the nontransfused controls. Mice rendered thrombocytopenic 48 hr earlier by antiplatelet serum, had 2-day 35S uptakes over 2 1/2 times the controls and 6 times the hypertransfused animals. The administration of a total of 2 ml of serum, given twice daily for 3 days from a thrombocytopenic patient with Hodgkin's disease caused a highly significant 103% rise in radiosulfate incorporation when compared with saline in the hypertransfused mouse. Normal human serum from a healthy donor caused a small and insignificant rise. The serum from a patient with Hodgkin's disease caused a highly significant 63% rise in 35S incorporation when compared to the normal serum.

scholarly journals Group IIA-Secreted Phospholipase A2in Human Serum Kills Commensal but Not ClinicalEnterococcus faeciumIsolates

2018 ◽  
Vol 86 (8) ◽  
Author(s):  
Fernanda L. Paganelli ◽  
Helen L. Leavis ◽  
Samantha He ◽  
Nina M. van Sorge ◽  
Christine Payré ◽  
...  
Keyword(s):  
Human Serum ◽  
Normal Serum ◽  
Gram Negative Bacteria ◽  
Opportunistic Pathogens ◽  
Gram Positive ◽  
Content Type ◽  
Gram Positive Bacteria ◽  
Normal Human ◽  
Direct Killing ◽  
The Complement System

ABSTRACTHuman innate immunity employs cellular and humoral mechanisms to facilitate rapid killing of invading bacteria. The direct killing of bacteria by human serum is attributed mainly to the activity of the complement system, which forms pores in Gram-negative bacteria. Although Gram-positive bacteria are considered resistant to killing by serum, we uncover here that normal human serum effectively killsEnterococcus faecium. Comparison of a well-characterized collection of commensal and clinicalE. faeciumisolates revealed that human serum specifically kills commensalE. faeciumstrains isolated from normal gut microbiota but not clinical isolates. Inhibitor studies show that the human group IIA secreted phospholipase A2 (hGIIA), but not complement, is responsible for killing of commensalE. faeciumstrains in human normal serum. This is remarkable since the hGIIA concentration in “noninflamed” serum was considered too low to be bactericidal against Gram-positive bacteria. Mechanistic studies showed that serum hGIIA specifically causes permeabilization of commensalE. faeciummembranes. Altogether, we find that a normal concentration of hGIIA in serum effectively kills commensalE. faeciumand that resistance of clinicalE. faeciumto hGIIA could have contributed to the ability of these strains to become opportunistic pathogens in hospitalized patients.

scholarly journals PRIMARY SERUM TOXICITY AS DEMONSTRATED BY THE CHICKEN EMBRYO

1935 ◽  
Vol 61 (4) ◽  
pp. 489-499 ◽  
Author(s):  
Ernst Witebsky ◽  
Erwin Neter
Keyword(s):  
Guinea Pig ◽  
Human Serum ◽  
Test Object ◽  
Chicken Embryo ◽  
Normal Serum ◽  
Vascular Network ◽  
Inhibitory Influence ◽  
Suitable Test ◽  
Forssman Antigen ◽  
Normal Human

1. The 3 day old chicken embryo removed from its shell is a suitable test object for the demonstration of primary serum toxicity. Addition of normal rabbit type sera as well as Forssman antiserum causes the vascular network to contract and the embryo sinks in the yolk and dies. 2. Only sera of animals of the so called rabbit type produce this phenomenon. Sera of the guinea pig type are ineffective. 3. Heating to 51°C. destroys the complement content of normal human serum as also its effectiveness to produce the vascular phenomenon. 4. Up to the present it has not been possible to reactivate heat-inactivated normal serum by the addition of complement, while inactivated Forssman antiserum can be easily reactivated. 5. The vascular phenomenon of the chicken embryo is produced not only by the addition of a mixture of Forssman antiserum and complement but also by separate addition of both components. 6. Guinea pig type sera, containing dissolved Forssman antigen, are not only ineffective but actually exert an inhibitory influence on effective rabbit type sera as well as on Forssman antiserum.

scholarly journals Group IIA secreted phospholipase A2in human serum kills commensal but not clinicalEnterococcus faeciumisolates

2018 ◽  
Author(s):  
Fernanda L. Paganelli ◽  
Helen L. Leavis ◽  
Samantha He ◽  
Nina M. van Sorge ◽  
Christine Payré ◽  
...  
Keyword(s):  
Human Serum ◽  
Enterococcus Faecium ◽  
Opportunistic Infections ◽  
Normal Serum ◽  
Gram Negative Bacteria ◽  
Gram Positive ◽  
Gram Negative ◽  
Gram Positive Bacteria ◽  
Serum Killing ◽  
Normal Human

AbstractHuman innate immunity employs cellular and humoral mechanisms to facilitate rapid killing of invading bacteria. The direct killing of bacteria by human serum is mainly attributed to the activity of the complement system that forms pores in Gram-negative bacteria. Although Gram-positive bacteria are considered resistant to serum killing, we here uncover that normal human serum effectively killsEnterococcus faecium.Comparison of a well-characterized collection of commensal and clinicalE. faeciumisolates revealed that human serum specifically kills commensalE. faeciumstrains isolated from normal gut microbiota, but not clinical isolates. Inhibitor studies show that the human group IIA secreted phospholipase A2 (hGIIA), but not complement, is responsible for killing of commensalE. faeciumstrains in human normal serum. This is remarkable since hGIIA concentrations in ‘non-inflamed’ serum were considered too low to be bactericidal against Gram-positive bacteria. Mechanistic studies showed that serum hGIIA specifically causes permeabilization of commensalE. faeciummembranes. Altogether, we find that a normal serum concentration of hGIIA effectively kills commensalE. faeciumand that hGIIA resistance of clinicalE. faeciumcould have contributed to the ability of these strains to become opportunistic pathogens in hospitalized patients.ImportanceHuman normal serum contains antimicrobial components that effective kill invading Gram-negative bacteria. Although Gram-positive bacteria are generally considered resistant to serum killing, here we show that normal human effectively kills the Gram-positiveEnterococcus faeciumstrains that live as commensals in the gut of humans. In contrast, clinicalE. faeciumstrains that are responsible for opportunistic infections in debilitated patients are resistant against human serum. The key factor in serum responsible for killing is group IIA secreted phospholipase A2 (hGIIA) that effectively destabilizes commensalE. faeciummembranes. We believe that hGIIA resistance by clinicalE. faeciumcould have contributed to the ability of these strains to cause opportunistic infections in hospitalized patients. Altogether, understanding mechanisms of immune defense and bacterial resistance could aid in further development of novel anti-infective strategies against medically important multidrug resistant Gram-positive pathogens.

scholarly journals Studies in Bisalbuminemia: Binding Properties of the Two Albumins

Blood ◽  
1962 ◽  
Vol 20 (2) ◽  
pp. 156-164 ◽  
Author(s):  
EDWARD J. SARCIONE ◽  
C. WILLIAM AUNGST
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Serum Protein ◽  
Serum Proteins ◽  
Protein Pattern ◽  
Total Serum ◽  
Binding Properties ◽  
Normal Human ◽  
Serum Components

Abstract 1. An abnormal serum protein pattern in a patient with Wegener’s granulomatosis and five of his relatives was identified as bisalbuminemia by electrophoretic and immunochemical methods. 2. With the exception of the patient with Wegener’s syndrome, the presence of bisalbuminemia was not associated with a significant change in total serum proteins, total albumin, serum components other than albumin, or any disease. 3. Addition of I131-thyroxine to bisalbumin sera resulted in thyroxine binding by albumin B but not by albumin A. The failure of albumin A to bind added I131-thyroxine leads to speculation that, in this family, neither albumin A nor B are identical to normal human serum albumin.

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