Glomerular Permeability to High Molecular Weight Dextrans in Acute Ischaemic Renal Failure and Postural Proteinuria

1970 ◽  
Vol 38 (1) ◽  
pp. 93-99 ◽  
Author(s):  
Pamela R. MacLean ◽  
J. J. B. Petrie ◽  
J. S. Robson
Keyword(s):  
Molecular Weight ◽  
Renal Failure ◽  
High Molecular Weight ◽  
Plasma Protein ◽  
Healthy Subjects ◽  
Plasma Proteins ◽  
Normal Subjects ◽  
Glomerular Permeability ◽  
Molecular Weight Range ◽  
Postural Proteinuria

1. Renal permeability to dextran of a molecular weight range approximating to that of the plasma proteins has been studied in six patients with acute ischaemic renal failure, four patients with postural proteinuria and six healthy subjects. 2. Results are expressed in terms of dextran selectivity indices which relate the clearance of dextran to its molecular weight. Indices of dextran selectivity were found to be high in acute ischaemic renal failure, postural proteinuria and in normal subjects. Comparable indices of plasma protein selectivity in these groups were low. 3. It is suggested that in postural proteinuria and acute ischaemic renal failure the proteinuria is not glomerular in origin, and that in these conditions macromolecules are filtered quite normally and urinary protein arises from a post glomerular source characterized by a lack of selectivity.

Homocysteinylation score of high-molecular weight plasma proteins

Amino Acids ◽  
2013 ◽  
Vol 46 (4) ◽  
pp. 893-899 ◽  
Author(s):  
Alexandr A. Zhloba ◽  
Tatiana F. Subbotina
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Plasma Proteins

Structure and Solution Properties of High Molecular Weight Butadiene-Styrene Copolymers

1957 ◽  
Vol 30 (1) ◽  
pp. 315-325
Author(s):  
R. B. MacFarlane ◽  
L. A. McLeod
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Complex Structure ◽  
Mixed Solvents ◽  
Solution Time ◽  
Solution Viscosity ◽  
Solution Properties ◽  
Molecular Weight Range ◽  
Viscosity Measurements ◽  
Commercial Practice

Abstract Production of high molecular weight copolymers of butadiene and styrene for use in oil-extended rubbers has aroused interest in the solution properties of copolymers above the molecular weight range commonly encountered in commercial practice. It has been observed that solubility of such polymers in toluene is a time-dependent phenomenon and the apparent solubility can increase continuously, in the absence of agitation, for as long as 800 hours. Although a standard Harris cage solubility test may show the presence of 50% gel, other properties do not confirm the presence of any appreciable quantities of insoluble material. Mild agitation rapidly promotes almost complete solubility. Dilute solution viscosity measurements are very misleading unless the influence of solution time is recognized and apparent intrinsic viscosities rise progressively with time of contact of the sample with solvent. This time-dependence of solution has been found to occur at conversions higher than 50% and is also a function of the amount of modifier used in the polymerization recipe. It has not been possible to shorten the solution time for viscosity measurements by mild heating or gentle agitation. Mixed solvents cause a change in the amount of increase of the apparent intrinsic viscosity but do not shorten the time to equilibrium. Measurement of the slope constant in the Huggins viscosity equation indicate that these solubility and viscosity effects coincide with the appearance of a marked degree of branching in the polymer molecules. The effect is, therefore, interpreted as being caused by the relatively slow disentanglement of molecules of complex structure.

scholarly journals Lab-on-a-Chip method uncertanties in determination of high-molecular-weight glutenin subunits

2013 ◽  
Vol 19 (4) ◽  
pp. 553-561 ◽  
Author(s):  
Dragan Zivancev ◽  
Branislava Nikolovski ◽  
Aleksandra Torbica ◽  
Jasna Mastilovic ◽  
Nevena Djukic
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Wheat Variety ◽  
Lab On A Chip ◽  
Good Resolution ◽  
Glutenin Subunits ◽  
Bread Making ◽  
Molecular Weight Range ◽  
Essential Information ◽  
Significant Difference

Polymeric wheat endosperm proteins, especially the high-molecular-weight glutenin subunits (HMW-GS), are probably the most interesting protein fraction giving the essential information about bread-making quality of wheat flour. A relatively new method that shows a great potential for a fast, reliable and automatable analysis of protein purity, sizing and quantification is microfluidic or Lab-on-a-Chip (LoaC) capillary electrophoresis. This work was aimed to explore the possibilities of implementation of LoaC method to analysis of protein samples isolated from a Serbian common wheat variety, emphasizing the steps that might bring uncertainties and affect reproducibility of obtained glutenin subunits quantitation results. A good resolution of protein bands in a molecular weight range of 14.0 to 220.0 kDa was achieved. The reproducibility of HMW-GS sizing and quantitation were good, with the average coefficient of variation values of 1.2% and 12.2%. The ratio of HMW-GS to low-molecular-weight glutenin subunits (LMW-GS) was about 20%. The investigation ruled out influences of the extract solution addition and the buffer addition steps of the applied method, as well as the individual chip influence on GS quantitation results. However, there was statistically significant difference between HMW-GS quantitation results of multi-step and one-step extraction procedures applied prior to glutenin subunits extraction step.

Hypoxia alters blood coagulation during acute decompression in humans

1984 ◽  
Vol 56 (3) ◽  
pp. 666-670 ◽  
Author(s):  
H. M. O'Brodovich ◽  
M. Andrew ◽  
G. W. Gray ◽  
G. Coates
Keyword(s):  
Molecular Weight ◽  
Platelet Count ◽  
Blood Coagulation ◽  
High Molecular Weight ◽  
Plasma Protein ◽  
Partial Thromboplastin Time ◽  
Activated Partial Thromboplastin Time ◽  
Total Plasma ◽  
High Molecular Weight Kininogen ◽  
Total Plasma Protein

Acute decompression is associated with a shortening of the activated partial thromboplastin time (aPTT). This study was performed to examine whether this change in aPTT results from hypoxia or hypobaria. We exposed healthy adults on three separate occasions to 2 h of 1) hypoxic hypobaria (410 Torr, n = 5), 2) hypoxic normobaria (fractional inspired O2 tension = 0.11, n = 4), or 3) normoxic hypobaria (410 Torr breathing supplemental O2, n = 5). The aPTT shortened during hypoxic hypobaria and hypoxic normobaria (P less than 0.05) but was unchanged during normoxic hypobaria. The prothrombin and thrombin times, hematocrit, and concentrations of fibrinogen, total plasma protein, and fibrinogen-fibrin fragment E were unchanged. During hypoxic hypobaria biologic levels of prekallikrein, high-molecular-weight kininogen, and factors XII, XI, X, VII, V, and II were unchanged, but procoagulant VIII (VIII:C) increased 50% without an increase in VIII-related antigen levels (VIIIR:Ag). Fibrin monomer was not detected in any group. In one subject who became ill after 1.5 h of hypoxic normobaria aPTT shortened by 10 s; the platelet count decreased by 93,000/mm3; VIII:C increased fivefold, but VIIIR:Ag only increased three-fold. We conclude that it is the hypoxia which shortens aPTT during acute decompression to 410 Torr and speculate that it results from an increase in plasma VIII:C-like activity.

scholarly journals Quantitative Abnormalities of Aα Chain Molecular Weight in the Fibrinogen of Cirrhotic Patients

1977 ◽  
Author(s):  
Mark Weinstein ◽  
Daniel Deykin
Keyword(s):  
Molecular Weight ◽  
Plasma Proteins ◽  
Normal Subjects ◽  
Small Samples ◽  
Two Stage ◽  
Large Pore ◽  
Total Range ◽  
Cirrhotic Patients ◽  
Electrophoretic Procedure ◽  
Molecular Weight Heterogeneity

A novel two-stage SDS gel electrophoretic procedure was devised to examine the molecular weight heterogeneity of fibrinogen in small samples of whole plasma from 12 normal and 7 cirrhotic individuals. Fibrinogen was first separated from other plasma proteins on a large pore gel, cut out of the gel, reduced, and separated into its component Aα, Bβ, and γ chains on a second gel. Two major mol wt species—fibrinogen I and II—were observed on the first gel. The ~ 25000 mol wt difference between these two forms reflected a decrease primarily in the size of one of the fibrinogen II Aα chains. In both normals and cirrhotic patients fibrinogen II comprised 30% of the total (range 20–35%). Fibrinogen I and II each contained two major high mol wt Aα chains—Aα/1 and a smaller Aα/2—that differ by 3000 mol wt. In normal fibrinogen I, Aα/2 comprised 33% of the total Aα chains (range 27–41%). In contrast the fibrinogen I of 6 out of the 7 patients had a lower per cent of Aα/2 (range 10–25%). Similar quantitative differences were seen in the decreased fraction of Aα/2 in the fibrinogen II of cirrhotic patients compared to normals. No correlation was found between per cent fibrinogen II and per cent Aα/2 in either normal subjects or cirrhotics. These results suggest that at least two independent processes are responsible for the observed levels of Aα chain heterogeneity in normals and cirrhotics and that one of these processes yields a lower than normal fraction of Aa/2 chains in the fibrinogen of cirrhotic individuals.

Monoclonal antibodies reveal circulating growth hormone of high molecular weight not detectable by conventional assays

1990 ◽  
Vol 123 (3) ◽  
pp. 317-325 ◽  
Author(s):  
Marguerite Luthman ◽  
Ingileif Jónsdóttir ◽  
Bo Skoog ◽  
Inga-Lena Wivall ◽  
Paul Roos ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Growth Hormone ◽  
High Molecular Weight ◽  
Specific Binding ◽  
Affinity Purification ◽  
Normal Subjects ◽  
Polyclonal Antiserum ◽  
Placental Lactogen ◽  
Gh Secretion ◽  
High Molecular Weight Proteins

Abstract. A radioimmunoassay based on a monoclonal antibody, Mc-ab 1, which was raised against growth hormone but cross-reacted with human placental lactogen yielded higher GH immunoreactivity levels in serum than one based on a polyclonal antiserum. This discrepancy was noted in subjects with normal GH secretion as well as in patients with GH insufficiency. To characterize this GH immunoreactivity detected by Mc-ab 1, affinity purification and molecular sieve chromatography of serum were performed. High molecular weight proteins with GH immunoreactivity were found with both techniques. These proteins were associated with carbohydrates. Affinity cross-linking showed specific binding of radiolabelled GH to high molecular weight proteins in the serum. After fractionation of serum, the GH immunoreactivity became detectable by the polyclonal antiserum assay as well as by an immunoradiometric assay. GH immunoreactive material with an approximate mass of 80 kD was subjected to isoelectric focusing. When GH immunoreactive fractions at pH 5 were re-chromatographed, GH immunoreactivity was recovered in the elution volume corresponding to monomeric GH. Our results show that sera from normal subjects as well as from patients with deficient GH secretion contain notable amounts of high molecular weight GH which is undetectable by antibodies generally used for GH measurements, but which can be revealed after fractionation of serum.

scholarly journals Real-time metabolic heat-based specific growth rate soft sensor for monitoring and control of high molecular weight HA production by Streptococcus zooepidemicus.

2020 ◽  
Author(s):  
Naresh Mohan ◽  
Satya Sai Pavan ◽  
Anjali Jayakumar ◽  
Sivakumar Rathinavelu ◽  
Senthilkumar Sivaprakasam
Keyword(s):  
Molecular Weight ◽  
Growth Rate ◽  
Specific Growth Rate ◽  
Real Time ◽  
High Molecular Weight ◽  
Specific Growth ◽  
Fed Batch ◽  
Molecular Weight Range ◽  
Weight Range ◽  
Metabolic Heat

Abstract Background: Hyaluronic acid (HA) is an important mucopolysaccharide of higher molecular weight range and holds sheer economic interest. Its applications are widely acknowledged in rheumatoid arthritis treatment, tissue engineering, and cosmetics industries. This present investigation aims for the fed-batch production of high molecular weight range HA by application of real-time metabolic heat measurements. Results: Fed-batch strategies based on Feedforward (FF) and Feedback (FB) control was devised to improve the Molecular Weight (MW) of HA production by S. zooepidemicus . Metabolic heat measurements (Fermentation calorimetry) were modeled to decipher real-time specific growth rate, [[EQUATION]] was looped to the PID circuit, envisaged to control [[EQUATION]] to their desired setpoint values 0.05 [[EQUATION]] , 0.1 [[EQUATION]] and 0.15 [[EQUATION]] respectively. The developed FB strategy established a robust control on maintaining the specific growth rate (µ) close to the [[EQUATION]] value with a minimal tracking error. Exponential feed rate carried out with a lowest [[EQUATION]] of 0.05 [[EQUATION]] improved the MW of HA significantly to 2.98 MDa and 2.94 MDa for the FF and FB based control strategies respectively. An optimal HA titer of 4.73 g/L was achieved in a FF control strategy at [[EQUATION]] . Biomass and Lactic acid (LA) concentrations were found to be concomitant with the increase in [[EQUATION]] from 0.05 [[EQUATION]] to 0.15 [[EQUATION]] . Superior control of µ at low [[EQUATION]] value was observed to influence positively the HA polymerization attributing to improved MW and desired Polydispersity Index (PDI) of HA. Conclusions: This present investigation attempts to address the metabolic bottleneck in synthesis of high MW HA by S. zooepidemicus and illustrates the application of calorimetric fed-batch control of µ at a narrower range. PID control offers advantage over conventional fed-batch method to synthesize HA at an improved MW. Calorimetric signal based µ control by PID negates adverse effects due to the secretion of other metabolites albeit maintaining homeostasis.

Plasma pancreatic trypsinogens in chronic renal failure and after nephrectomy

1982 ◽  
Vol 242 (2) ◽  
pp. G177-G182
Author(s):  
M. C. Geokas ◽  
R. Reidelberger ◽  
M. O'Rourke ◽  
E. Passaro ◽  
C. Largman
Keyword(s):  
Renal Failure ◽  
Chronic Renal Failure ◽  
Plasma Levels ◽  
Intravenous Infusion ◽  
Plasma Proteins ◽  
Plasma Concentrations ◽  
Normal Subjects ◽  
Cationic Trypsinogen ◽  
Anephric Patients ◽  
Highly Correlated

The kidney has previously been shown to be a major site for the plasma clearance of pancreatic trypsinogens in the rat. This study investigated plasma concentrations of anionic and cationic trypsinogen in chronic renal failure and anephric patients. Plasma concentrations were significantly elevated in both groups of patients. Hemodialysis did not change their plasma levels. The plasma levels of anionic and cationic trypsinogens were highly correlated in patients and normal subjects; however, the relative concentrations of anionic trypsinogen were significantly higher in renal failure patients. This suggests that in patients with renal failure the secondary clearance mechanisms for these plasma proteins more efficiently clear cationic molecules. In normal dogs, intravenous infusion of synthetic octapeptide of cholecystokinin (CCK-8) resulted in small transitory increases in plasma trypsinogen levels. After nephrectomy, basal levels of anionic and cationic trypsinogen were elevated, and intravenous infusion of CCK-8 resulted in prolonged, high levels of plasma trypsinogens.

Plasma Protein Oxidation Is Associated with an Increase of Procoagulant Markers Causing an Imbalance between Pro- and Anticoagulant Pathways in Healthy Subjects

2002 ◽  
Vol 87 (01) ◽  
pp. 58-67 ◽  
Author(s):  
Bianca Rocca ◽  
Roberto Marchioli ◽  
Raffaele Landolfi ◽  
Raimondo De Cristofaro
Keyword(s):  
Plasma Protein ◽  
Protein Oxidation ◽  
Healthy Subjects ◽  
Plasma Proteins ◽  
Protein C ◽  
Ex Vivo ◽  
Protein Carbonyl ◽  
Fibrinopeptide A ◽  
Carbonyl Content ◽  
Protein Carbonyl Content

SummaryThe aim of the present study was to investigate whether the overall oxidation state of plasma proteins is associated with changes of circulating pro- and anticoagulant markers in healthy subjects (n = 99, 49 males, 50 females, aged from 6 to 91 yrs.). The carbonyl content of plasma proteins was measured and validated as an ex vivo index of the overall protein oxidation state due to its correlation with the plasma level of o-tyrosine (r = 0.87, P <0.0001), which is a well known oxidized product of L-phenylalanine. Using a multivariate analysis the carbonyl content of plasma protein was positively associated with procoagulant markers such as prothrombin F1 + 2 (r = 0.28, P = 0.0019) and fibrinopeptide A, (FpA) (r = 0.278, P = 0.003), as well as with the soluble derivative of the endothelial protein thrombomodulin (TM) (r = 0.469, P <0.0001). The procoagulant marker of thrombin activity, FpA, was significantly and positively correlated with the anticoagulant product of thrombin, namely the Protein C activation peptide (PCP), only in the tertile with low protein carbonyl content. At higher tertiles this correlation was no longer observed, thus suggesting a detrimental effect of oxidative stress on the TM/Protein C anticoagulant pathway. In 15 subjects with high carbonyl content of plasma protein, treatment for 18 days with 600 mg/d of vitamin E did not substantially modify the protein carbonyl content, the anticoagulant markers APC/PCP, and all procoagulant markers except F1+2, whose value significantly decreased by 25%.In conclusion, the present study shows that a high plasma protein oxidation ex vivo is associated with an overall hemostatic imbalance, which favors procoagulant markers. Vitamin E treatment in vivo restores only in part the equilibrium between pro- and anticoagulant pathways. This may open the way to further studies aimed at elucidating the mechanisms by which the oxidative stress is linked to activation of the coagulation system in atherothrombotic disorders. Abbreviations: APC: activated Protein C; F1+2: prothrombin fragment 1+2; FpA: fibrinopeptide A; PCP: Protein C activation peptide; TM: thrombomodulin

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