Vasoactive properties of plasma protein fractions

1964 ◽  
Vol 206 (4) ◽  
pp. 923-925 ◽  
Author(s):  
M. Wurzel ◽  
R. C. Bacon ◽  
R. B. Kalt ◽  
B. W. Zweifach

The capacity of plasma to potentiate norepinephrine (NOR)-induced contractions of the rabbit aortic strip can be attributed to the plasma protein fractions, perhaps almost exclusively to their albumin content. Albumin, 0.2–2 mg/15 ml, potentiated a threshold test dose of NOR from minimal to maximal effect. In the presence of albumin 1–2 mg/15 ml, the threshold dose of NOR was decreased about five to ten times. Albumin, 500 mg/15 ml, did not have a greater potentiating effect. Albumin itself had no contracting ability. The blood of the anesthetized rabbit does not contain sufficient NOR to contract the aortic strip; such concentrations of NOR even in the presence of plasma proteins or albumin were ineffective. The data suggest that NOR does not contribute directly to the maintenance of normal vascular tone.

1949 ◽  
Vol 33 (2) ◽  
pp. 103-124 ◽  
Author(s):  
David Grob

1. Serum proteinase precursor was found in plasma protein fractions I and III of Cohn. Inhibitors of serum proteinase, leucoproteinase, trypsin, and papain were found in fractions IV-1 and IV-4, and to a lesser extent in fractions V and I. 2. Pancreatic, soy bean, lima bean, and egg white inhibitors inhibited trypsin stoichiometrically. Pancreatic inhibitor had comparable inhibitory activity against serum proteinase; soy bean inhibitor had somewhat less, lima bean inhibitor even less, and egg white inhibitor very little. None of these inhibitors appreciably inhibited leucoproteinase or papain. 3. Serum and fractions IV - 1 and IV - 4 had marked inhibitory activity against trypsin and leucoproteinase, and somewhat less against serum proteinase and papain. The inhibitory activity of the plasma proteins against trypsin and leucoproteinase was due almost entirely to fractions IV - 1 and IV - 4; against serum proteinase and papain fraction V was slightly more important. The "reconstituted plasma proteins" accounted for 8 to 25 per cent of the proteinase-inhibitory activity of whole serum or plasma. 4. The proteinase-inhibitory activity of serum, plasma protein fractions, and soy bean inhibitor was heat labile, while that of pancreatic, lima bean, and egg white inhibitors was relatively heat stable. 5. Reducing and oxidizing agents, in very high concentration, inhibited serum proteinase, as well as trypsin and leucoproteinase. These proteinases were not influenced by mercurial sulfhydryl inhibitors, indicating that free sulfhydryl groups do not play an important part in their activity.


2015 ◽  
Vol 49 (2) ◽  
pp. 89-94
Author(s):  
N Roohi ◽  
A Shaukat ◽  
MA Iqbal ◽  
T Mumtaz

Workers of textile industry are exposed to different hazardous chemicals that cause adverse effects on their health. As variations in plasma proteins are the best indicators of health status of the subjects, hence, we compared plasma protein fractions, resolved by SDS-PAGE of textile dyeing industry workers (n=30) with control subjects (n=30). Proteins were quantified by Total Lab Quant software and analyzed, statistically, by Student t-test. Thirteen protein fractions were detected ranging 250-17kDa. A significant increase in 132 and 53kDa fractions, whereas, a significant decrement in 87 and 66kDa fractions with a highly significant reduction in 112kDa fraction was observed. However, 250, 224, 43, 23, 19 and 17kDa protein fractions did not vary considerably. As some proteins circulate only during particular physiological or pathological circumstances and may serve as biomarkers of anomalies, the altered expressions of these biomolecules observed in textile dyeing industry workers may be strong predictors of different ailments. DOI: http://dx.doi.org/10.3329/bjsir.v49i2.22002 Bangladesh J. Sci. Ind. Res. 49(2), 89-94, 2014


1990 ◽  
Vol 258 (6) ◽  
pp. H1650-H1654
Author(s):  
N. A. Mortillaro ◽  
A. E. Taylor

Steady-state lymph flow and lymph (CL) and plasma (CP) protein concentrations were measured at venous outflow pressures of 0, 10, 20, and 30 mmHg in an autoperfused segment of cat jejunum. In addition to determining total protein concentrations in lymph and plasma, polyacrylamide gradient gel electrophoresis was used to determine lymph and plasma protein concentrations of albumin and nine other plasma proteins. The osmotic reflection coefficient (sigma d) for total proteins, albumin, and each of the nine protein fractions was estimated using CL/CP at a capillary filtration rate independent state, when 1 - CL/CP = sigma d. A sigma d of 0.83 was obtained for total proteins, a value similar to that reported for both dog jejunum and descending colon (0.85) but appreciably different from that reported for both cat stomach (0.78) and ileum (0.92). Additionally, sigma d for albumin and each of the nine plasma protein fractions (molecular radii ranging from 37 to 120 A) increased as molecular radius increased. A two-pore model composed of a ratio of 3,750 48-A radius small pores to one 250-A radius large pore describes the data obtained, with 82% of the total volume flow occurring through the small pores and 16% through the large pores.


1975 ◽  
Vol 66 (1) ◽  
pp. 42-59 ◽  
Author(s):  
C M Redman ◽  
D Banerjee ◽  
K Howell ◽  
G E Palade

Colchicine, both in vitro and in vivo, inhibits secretion of albumin and other plasma proteins. In vitro, secretion by rat liver slices is inhibited at 10-minus 6 M with maximal effect at 10-minus 5 M. Inhibition of secretion is accompanied by a concomitant retention of nonsecreted proteins within the slices. Colchicine does not inhibit protein synthesis at these concentrations. Vinblastine also inhibits plasma protein secretion but lumicolchicine, griseofulvin, and cytochalasin B do not. Colchicine also acts in vivo at 10-25 mumol/100 g body weight. Inhibition of secretion is not due to changes in the intracellular nucleotide phosphate levels. Colchicine, administered intravenously, acts within 2 min and its inhibitory effect lasts for at least 3 h. Colchicine has no effect on transport of secretory proteins in the rough or smooth endoplasmic reticulum but it causes these proteins to accumulate in Golgi-derived secretory vesicles.


Vox Sanguinis ◽  
1962 ◽  
Vol 7 (4) ◽  
pp. 406-413 ◽  
Author(s):  
E. H. Mealey ◽  
L. H. Larsen ◽  
R. C. Dwyer ◽  
D. J. Mulford

1935 ◽  
Vol 62 (3) ◽  
pp. 353-258 ◽  
Author(s):  
James B. McNaught ◽  
Francis M. Woods ◽  
Virgil Scott

A non-splenectomized dog, on a vitamin-adequate basal diet, in the course of a plasmapheresis experiment, developed an uncontrollable anemia associated with the presence of bodies in or on the erythrocytes, indistinguishable from the descriptions of Bartonella canis. The normal plasma protein level of 7.3 per cent was reduced to 4.1 per cent by diet and the removal of 5354 ml. of whole blood in 33 bleedings. The Bartonella infection was transferred to a splenectomized dog by an intravenous injection of whole blood. Each animal was apparently sterilized by one injection of neoarsphenamine equivalent to 15 mg. per kilo weight. It is possible that the spleen liberates some substance into the blood stream which has an inhibitory effect upon a latent Bartonella infection and that this protective substance was diminished by the many bleedings associated with the lowering of plasma proteins in the non-splenectomized dog and was lacking in the inoculated splenectomized dog.


1924 ◽  
Vol 39 (6) ◽  
pp. 921-929 ◽  
Author(s):  
G. C. Linder ◽  
C. Lundsgaard ◽  
D. D. Van Slyke ◽  
E. Stillman

1. We have not observed gross increases in plasma volume in glomerulonephritis, nephrosis, or nephrosclerosis, even when the concentration of plasma proteins was much below normal. Our results indicate the probability that "hydremic plethora" does not occur. 2. The low protein concentration frequently observed in the plasma in nephritis is not due to increased plasma volume but to a decrease of the total amount of plasma protein in the body. 3. Changes in plasma volume showed no constant relationship to changes in edema.


2009 ◽  
Vol 297 (4) ◽  
pp. E889-E897 ◽  
Author(s):  
Abdul Jaleel ◽  
Katherine A. Klaus ◽  
Dawn M. Morse ◽  
Helen Karakelides ◽  
Lawrence E. Ward ◽  
...  

It remains to be determined whether systemic insulin replacement normalizes synthesis rates of different plasma proteins and whether there are differential effects on various plasma proteins. We tested a hypothesis that insulin deprivation differentially affects individual plasma protein synthesis and that systemic insulin treatment may not normalize synthesis of all plasma proteins. We measured synthesis rates of 41 plasma proteins in seven each of type 1 diabetic (T1DM) and nondiabetic participants (ND) using [ ring-13C6]phenylalanine as a tracer. T1DM were studied while on chronic insulin treatment and during 8 h insulin deprivation. Insulin treatment normalized glucose levels, but plasma insulin levels were higher during insulin treatment than during insulin deprivation in T1DM and ND. Individual plasma proteins were purified by affinity chromatography and two-dimensional gel electrophoresis. Only 41 protein gel spots from over 300 were chosen based on their protein homogeneity. Insulin deprivation and hyperglycemia either significantly increased ( n = 12) or decreased ( n = 12) synthesis rates of 24 of 41 plasma proteins in T1DM compared with ND. Insulin treatment normalized synthesis rates of 13 of these 24 proteins, which were altered during insulin deprivation. However, insulin treatment significantly altered the synthesis of 14 additional proteins. In conclusion, acute insulin deprivation caused both a decrease and increase in synthesis rates of many plasma proteins with various functions. Moreover, chronic systemic insulin treatment not only did not normalize synthesis of all plasma proteins but also altered synthesis of several additional proteins that were unaltered during insulin deprivation.


1987 ◽  
Vol 35 (4) ◽  
pp. 521-524
Author(s):  
J.H. Boon ◽  
J.M. Smits ◽  
T. Wensing ◽  
E. Lo

The effect of feeding level and water supply on the total content of plasma protein (TPP) and fractions of these proteins (PPF) of young African catfish was studied. It was found that TPP can be divided into 4 fractions (PPF I-IV), of which PPF I is predominant. Analysis of the results showed a strong effect of feeding level on TPP and PPF I-IV. There was a positive correlation between TPP and the weights of PPF I-IV, and a negative correlation between PPF I and PPF II. The PPF I fraction might be usable as an indicator for the health status of young catfishes. (Abstract retrieved from CAB Abstracts by CABI’s permission)


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