MONOMER AND DIMER FORMS OF GAMMA-GLOBULIN POLYPEPTIDES IN NORMAL URINE

1964 ◽  
Vol 42 (12) ◽  
pp. 1815-1823 ◽  
Author(s):  
M. H. Freedman ◽  
G. E. Connell
Keyword(s):  
Molecular Weight ◽  
Disulfide Bonds ◽  
Gamma Globulin ◽  
The Other ◽  
Light Chains ◽  
Low Molecular Weight ◽  
Γ Globulins ◽  
Intermolecular Disulfide Bonds ◽  
Normal Urine ◽  
Polypeptide Chains

The γ-globulins of low molecular weight in human urine have been partially fractionated and characterized. The two principal components are made up of "light" polypeptide chains of 7 S γ-globulin. One of these components, the "monomer", has a molecular weight in dissociating solvents of approximately 20,000 and probably consists of single light chains. The other component, the "dimer", has a molecular weight of approximately 40,000 and probably consists of pairs of light chains joined by intermolecular disulfide bonds.

scholarly journals RECONSTITUTION OF 7S MOLECULES FROM L AND H POLYPEPTIDE CHAINS OF ANTIBODIES AND γ-GLOBULINS

1964 ◽  
Vol 119 (5) ◽  
pp. 789-815 ◽  
Author(s):  
D. E. Olins ◽  
G. M. Edelman
Keyword(s):  
Molecular Weight ◽  
Propionic Acid ◽  
Disulfide Bonds ◽  
Average Molecular Weight ◽  
Antigenic Structure ◽  
Hybrid Molecules ◽  
Different Types ◽  
Γ Globulins ◽  
Chain Fraction ◽  
Polypeptide Chains

Admixture of separated L and H polypeptide chains of 7S γ-globulins under appropriate conditions has been found to result in the reconstitution of 7S molecules. The chains were mixed in 0.5 N propionic acid and when dialyzed into neutral aqueous buffers interacted to form reconstituted material in greater than 30 per cent yield. This material had sedimentation coefficients of 6S to 7S, a weight average molecular weight of 160,000, and its antigenic structure and electrophoretic properties were the same as those of 7S γ-globulin. By the use of I131 and I125 labels on the different types of chains, combined with ultracentrifugation of chain mixtures in sucrose density gradients, the 7S product was found to contain both isotopes in ratios consistent with the presence of two L and two H chains. After hydrolysis with papain, the reconstituted material yielded products resembling S and F fragments. All of the isotope corresponding to L chains was found in the counterpart of the S fragment; the isotope corresponding to the H chain fraction was present in both fragments. The activity reconstituted from chains of a purified guinea pig antibody to f1 phage was found to be associated mainly with the 7S material. Hybrid molecules containing rabbit L chains and human H chains and of human L chains and rabbit H chains were formed by the same techniques of reconstitution. It was found that the interchain disulfide bonds of native 7S γ-globulins could be broken and reoxidized, as could those of reconstituted 7S material. Reduced L and H chains mixed in propionic acid, dialyzed against neutral buffers containing mercaptan, then against neutral buffers in the absence of mercaptan, formed stable 7S molecules of molecular weight 160,000, which were dissociable only after reduction.

scholarly journals ACTIVITY OF DISSOCIATED AND REASSOCIATED 19S ANTI-γ-GLOBULINS

1964 ◽  
Vol 120 (6) ◽  
pp. 1215-1229 ◽  
Author(s):  
Ralph E. Schrohenloher ◽  
Henry G. Kunkel ◽  
Thomas B. Tomasi
Keyword(s):  
Rheumatoid Arthritis ◽  
Molecular Weight ◽  
Disulfide Bonds ◽  
Red Cells ◽  
Low Molecular Weight ◽  
Density Gradient Ultracentrifugation ◽  
High State ◽  
Analytical Ultracentrifuge ◽  
Γ Globulins ◽  
Molecular Weight Fractions

19S anti-γ-globulins were isolated in a high state of purity from the sera of two patients with rheumatoid arthritis. Following reduction with ethyl mercaptan and alkylation by iodoacetamide, fragments were produced which retained the capacity to combine with 7S γ-globulin. The fragments from one of the 19S anti-γ-globulins agglutinated red cells coated with incomplete anti-Rh antibodies. This activity was shown by density gradient ultracentrifugation to be associated with low molecular weight fractions. The agglutination of the coated red cells by the fragments was strongly inhibited by normal and myeloma 7S γ-globulins and showed a greater specificity than the parent 19S material. Analytical ultracentrifuge experiments demonstrated that the fragments from either of the 19S anti-γ-globulins formed complexes with 7S γ-globulin. Reassociation of the dissociated fragments through reformation of disulfide bonds resulted in the formation of fast sedimenting molecules having properties similar to those of the untreated 19S material in respect to precipitation with aggregated γ-globulin and agglutination of coated red cells.

THE HETEROGENEITY OF GAMMA-GLOBULIN IN POST-EXERCISE URINE

1964 ◽  
Vol 42 (7) ◽  
pp. 1065-1097 ◽  
Author(s):  
M. H. Freedman ◽  
G. E. Connell
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Polypeptide Chain ◽  
Gel Filtration ◽  
Low Molecular Weight ◽  
Starch Gel Electrophoresis ◽  
Single Individual ◽  
Post Exercise ◽  
Γ Globulins ◽  
Normal Urine

Post-exercise urine was collected and the protein was precipitated with ammonium sulphate. The γ-globulin was separated from other urinary proteins by preparative starch block electrophoresis. The γ-globulin was then separated by gel filtration into two fractions, the faster one consisting mainly of 7 S γ-globulin while the slower one contained "low molecular weight" γ-globulin sedimenting at 3.5 S. The low molecular weight γ-globulins were further fractionated on CM-Sephadex to yield four fractions. Each of the chromatographic fractions was shown to be heterogeneous by starch gel electrophoresis at pH 4. The same degree of heterogeneity was observed in preparations of pooled urinary γ-globulin and γ-globulin from a single individual. The two major electrophoretic components of each chromatographic fraction formed precipitates in agar diffusion tests with antiserum to 7 S γ-globulin and to the L-polypeptide chain of 7 S γ-globulin. Two chromatographic fractions reacted with antiserum to the H-polypeptide chain of 7 S γ-globulin. All of the fractions failed to react with antiserum to β2A-globulin and β2M-globulin. Amino acid analysis showed distinct differences among the chromatographic fractions. One of the fractions closely resembled the L-chain of 7 S plasma γ-globulin with respect to amino acid composition. After reduction of disulphide bonds and alkylation most of the urinary γ-globulin resembles L-chain in electrophoretic behavior. The γ-globulins of post-exercise urine were found to be qualitatively similar to the γ-globulins of normal urine but post-exercise γ-globulins were present quantitatively in much larger amounts.

The Kidney and Fibrinolysis

1970 ◽  
Vol 24 (01/02) ◽  
pp. 026-032 ◽  
Author(s):  
N. A Marsh
Keyword(s):  
Molecular Weight ◽  
Plasminogen Activator ◽  
Enzyme System ◽  
Normal Animal ◽  
Fibrinolytic Enzyme ◽  
The Other ◽  
Exclusion Chromatography ◽  
Normal Urine ◽  
Renal Origin ◽  
Molecular Exclusion Chromatography

SummaryMolecular exclusion chromatography was performed on samples of urine from normal and aminonucleoside nephrotic rats. Normal urine contained 2 peaks of urokinase activity, one having a molecular weight of 22,000 and the other around 200,000. Nephrotic urine contained three peaks of activity with MW’s 126,000, 60,000 and 30,000. Plasma activator determined from euglobulin precipitate had a MW. in excess of 200,000. The results indicate that in the normal animal, plasma plasminogen activator does not escape into the urine in substantial quantities but under the conditions of extreme proteinuria there may be some loss through the kidney. The alteration in urokinase output in nephrotic animals indicates a greatly disordered renal fibrinolytic enzyme system.The findings of this study largely support the hypothesis that plasma plasminogen activator of renal origin and urinary plasminogen activator (urokinase) are different molecular species.

scholarly journals Bridge-therapy with enoxaparin in the preoperative period of endarterectomy

2010 ◽  
Vol 68 (5) ◽  
pp. 775-777
Author(s):  
Jair Leopoldo Raso ◽  
Rogério Zenóbio Darwich ◽  
Francisco de Lucca Jr ◽  
Romeu Valle Santana ◽  
Marco Túlio Tanure ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Mortality Rate ◽  
Prospective Study ◽  
Low Molecular Weight Heparin ◽  
The Other ◽  
Low Molecular Weight ◽  
Preoperative Period ◽  
Safe Strategy ◽  
A Prospective Study ◽  
Bridge Therapy

Cervical clot is one of the complications of endarterectomy. This risk may be higher in patients using aspirin or clopidogrel. On the other hand, stroke may occur if the medication is interrupted before surgery. We carried out a prospective study of 124 endarterectomies in 119 patients in which aspirin or clopidogrel was stopped and a bridge-therapy with enoxaparin was administered preoperatively. There was no case of stroke during the period of the bridge-therapy. One patient developed cervical clot (0.8%) in the fifth postoperative day. Mortality rate in this series was 0.8%. There was no complication directly related to the use of enoxaparin. Bridge-therapy with low molecular weight heparin is a safe strategy for patients elected for endarterectomy

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.

In Vitro Characterization Of Low Molecular Weight Fractions Of Heparin

1981 ◽  
Author(s):  
Jawed Fareed ◽  
Harry L Messmore ◽  
Daniel A Walz ◽  
Jean Choay ◽  
J C Lormeau
Keyword(s):  
Molecular Weight ◽  
The Other ◽  
Low Molecular Weight ◽  
In Vitro Test ◽  
Thrombin Time ◽  
Specific Test ◽  
Platelet Factor ◽  
At Iii ◽  
Heparin Fractions

Numerous extraction, chromatographic (ion exchange, gel, and affinity), chemical and enzymatic degradation methods have been employed to obtain heparin fractions. The present assays to evaluate potency (e.g. pharmacopeial and coagulant) do not truly reflect the antithrombotic properties of these fractions. In addition, the synthetic peptide substrate based assays to measure the anti Xa activity do not correlate with the coagulant anti Xa assays. We have developed an in vitro test battery to evaluate low molecular weight heparin fractions. Porcine mucosal heparin fractions are assayed for anti Xa activity in coagulant and amidolytic assays and the results are expressed as a ratio. The effect of these fractions on coagulant assays such as prothrombin time (PT), partial thromboplastin time (PTT), thrombin time (TT), Stypven time (ST) on freshly prepared normal human plasma (NHP) is determined The retention characteristics of these fractions on platelet factor 4 and AT-III bound sepharose columns were also determined. We have compared the extracted and chemically depolymerized heparin fractions and found that the anti Xa activity doesn’t always correlate with the other parameters studied. The extracted fractions were slightly stronger in the USP assays and showed a biphasic retention on the PF-4 column whereas the chemically depolymerized product showed only one peak. On the other hand, on the AT-III column both fractions showed similar elution patterns. Our studies suggest that heparin and its fractions exhibit differential behavior on various assays and a specific test may not be used as an index of the potency of their antithrombotic effects. Furthermore, the potency of these fractions should be stated on a weight basis when evaluated in the in vivo animal models rather than in terms of a specific test (e.g. anti Xa activity and US Pharmacopeial assays).

STUDIES ON THE ISOLATION AND NATURE OF THE 'TERREGENS FACTOR'

1954 ◽  
Vol 32 (1) ◽  
pp. 400-406 ◽  
Author(s):  
M. O. Burton ◽  
F. J. Sowden ◽  
A. G. Lochhead
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Ferric Iron ◽  
Test Organism ◽  
The Other ◽  
Inorganic Salts ◽  
Low Molecular Weight ◽  
Straight Chain ◽  
Heat Stable ◽  
Growth Promoting

A procedure is described for the production and concentration of the 'terregens factor' (TF), a bacterial growth promoting substance synthesized by Arthrobacter pascens and essential for the growth of Arthrobacter terregens. From culture filtrates of A. pascens cultivated in a medium of inorganic salts and sucrose, concentrates of TF may be obtained that are active at 0.001 μgm. Per ml., heat stable and contain about 12.7% nitrogen. Acid hydrolysis yielded a number of amino acids, including glutamic acid, glycine, α–alanine, valine, leucine, proline, lysine, and arginine, as well as some unidentified compounds; however, TF does not appear to be a low molecular weight straight chain peptide.Although TF contains no iron, it combines readily with ferrous or ferric iron to form reddish-brown complexes with this metal. Activity for A. terregens is shown by certain iron containing complexes as hemin, coprogen, and ferrichrome. On the other hand none is shown by cytochrome or pulcherrimin; however, aspergillic acid, structurally related to the latter, possesses some growth promoting activity for the test organism.

scholarly journals Viscoelastic Properties of Unentangled Multicyclic Polystyrenes

Polymers ◽  
2018 ◽  
Vol 10 (9) ◽  
pp. 973 ◽  
Author(s):  
Zhi-Chao Yan ◽  
Md. Hossain ◽  
Michael Monteiro ◽  
Dimitris Vlassopoulos
Keyword(s):  
Molecular Weight ◽  
Shear Viscosity ◽  
Viscoelastic Properties ◽  
Dilution Effect ◽  
The Other ◽  
Low Molecular Weight ◽  
Zero Shear Viscosity ◽  
Rouse Model ◽  
Loop Size ◽  
Linear Chains

We report on the viscoelastic properties of linear, monocyclic, and multicyclic polystyrenes with the same low molecular weight. All polymers investigated were found to exhibit unentangled dynamics. For monocyclic polymers without inner loops, a cyclic-Rouse model complemented by the contribution of unlinked chains (whose fraction was determined experimentally) captured the observed rheological response. On the other hand, multicyclic polymers with inner loops were shown to follow a hierarchical cyclic-Rouse relaxation with the outer loops relaxing first, followed by the inner loop relaxation. The influence of unlinked linear chains was less significant in multicyclic polymers with inner loops. The isofrictional zero-shear viscosity decreased with increasing number of constrained segments on the coupling sites, which was attributed to the decreasing loop size and the dilution effect due to the hierarchical relaxation.

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.

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