Studies on Acute Phase Proteins of Rat Serum. I. Isolation and Partial Characterization of an α1-Acid Glycoprotein and an α2-Macroglobulin

1972 ◽  
Vol 50 (8) ◽  
pp. 856-870 ◽  
Author(s):  
J. C. Jamieson ◽  
A. D. Friesen ◽  
F. E. Ashton ◽  
B. Chou
Keyword(s):  
Molecular Weight ◽  
Physical Properties ◽  
Acute Phase ◽  
Isoelectric Point ◽  
Acute Phase Proteins ◽  
Partial Characterization ◽  
Rat Serum ◽  
Acid Glycoprotein ◽  
Α2 Macroglobulin

An α1-acid glycoprotein and an α2-macroglobulin were isolated from serum from rats suffering from experimentally induced inflammation for 48 h. The proteins were characterized electrophoretically and immunologically and their carbohydrate compositions and some physical properties determined. The α1-acid glycoprotein contained 34.1% carbohydrate, had an isoelectric point of 2.95, and a molecular weight of 43 000. The α2-macroglobulin contained 15.9% carbohydrate, had an isoelectric point of 4.60, and a molecular weight of about 800 000. The properties of the two proteins are compared with those of similar proteins isolated from rats and other species.

Studies on Acute Phase Proteins of Rat Serum. II. Determination of the Contents of α1-Acid Glycoprotein, α2-Macroglobulin, and Albumin in Serum from Rats Suffering from Induced Inflammation

1972 ◽  
Vol 50 (8) ◽  
pp. 871-880 ◽  
Author(s):  
J. C. Jamieson ◽  
F. E. Ashton ◽  
A. D. Friesen ◽  
B. Chou
Keyword(s):  
Acute Phase ◽  
Acute Phase Proteins ◽  
Rat Serum ◽  
Experimental Animals ◽  
Acid Glycoprotein ◽  
Inflammatory Agent ◽  
Glycoprotein Biosynthesis ◽  
Α2 Macroglobulin

A quantitative precipitin technique has been employed to determine the contents of α1-acid glycoprotein, α2-macroglobulin, and albumin in serum from control rats and rats suffering from induced inflammation for 5–96 h. There was an increase in the content of α1-acid glycoprotein and α2-macroglobulin in serum from experimental animals reaching a maximum at 48–72 h after administration of inflammatory agent indicating that both proteins are acute phase globulins. There was only a slight change in the content of albumin in serum from experimental animals when compared with controls. Studies involving incorporation of labelled precursors of glycoprotein biosynthesis into α1-acid glycoprotein and α2-macroglobulin indicated that the most likely explanation for the increase in α1-acid glycoprotein and α2-macroglobulin in serum from experimental animals was an increase in the rates of synthesis of the two proteins in question.

Studies on Acute Phase Proteins of Rat Serum. V. Effect of Induced Inflammation on the Synthesis of Albumin and α1-Acid Glycoprotein by Liver Slices

1975 ◽  
Vol 53 (4) ◽  
pp. 401-414 ◽  
Author(s):  
J. C. Jamieson ◽  
K. E. Morrison ◽  
D. Molasky ◽  
B. Turchen
Keyword(s):  
Acute Phase ◽  
Polypeptide Chain ◽  
Serum Proteins ◽  
Acute Phase Proteins ◽  
Rat Serum ◽  
Acid Glycoprotein ◽  
Liver Slices ◽  
Microsome Fraction ◽  
Lower Capacity ◽  
Acute Phase Serum

Liver slices from normal rats and those suffering from inflammation for 24–48 h were incubated with L-[14C]leucine or D-[I4C]glucosamine. Immunological techniques coupled with radioautography indicated that the microsome fraction prepared from slices contained the subcellular site of synthesis of the polypeptide chain of serum albumin, and the polypeptide and carbohydrate chains of α1-acid glycoprotein; both proteins were also present in the medium in labelled forms. The contents of albumin and α1-acid glycoprotein in the medium and in extracts of liver from experiments with liver slices from control rats and 8–72 h experimental rats were determined using the quantitative precipitin technique. There was a net increase in synthesis of both proteins when slices from control and experimental animals were used, the increase showing up in medium proteins. However, slices from livers from 8–72 h experimental rats had a greater capacity for synthesis of α1-acid glycoprotein and a lower capacity for synthesis of albumin than slices from livers from control rats, the greatest changes occurring with slices from 24 h experimental rats. Changes in synthetic capacities of liver slices from experimental rats for albumin and α1-acid glycoprotein were always accompanied by large increases in specific radioactivities of total medium proteins when experiments involved incubation of slices with L-[3H]leucine and D-[14C]glucosamine. It is suggested that the increase in specific radioactivities of medium proteins following incubation of liver slices from experimental rats with labelled leucine and glucosamine is a characteristic of the response of liver to inflammation, and reflects changes in the capacity of liver for the synthesis of α1-acid glycoprotein and other acute phase serum proteins.

Studies on Acute Phase Proteins of Rat Serum. IV. Pathway of Secretion of Albumin and α1-Acid Glycoprotein from Liver

1973 ◽  
Vol 51 (9) ◽  
pp. 1281-1291 ◽  
Author(s):  
J. C. Jamieson ◽  
F. E. Ashton
Keyword(s):  
Endoplasmic Reticulum ◽  
Acute Phase ◽  
Rough Endoplasmic Reticulum ◽  
Golgi Complex ◽  
Acute Phase Proteins ◽  
Smooth Endoplasmic Reticulum ◽  
Rat Serum ◽  
Experimental Animals ◽  
Acid Glycoprotein ◽  
Ionic Detergent

Normal rats and those suffering from inflammation for 12 h were given pulse injections of L-leucine-3H and D-glucosamine-14C and were killed at 3–60 min thereafter. Rough and smooth microsome fractions and a Golgi-enriched fraction were prepared from liver and the fractions were extracted with the non-ionic detergent Lubrol-W. Albumin and acute phase α1-acid glycoprotein were isolated from the extracts by application of a quantitative precipitin technique employing antisera to albumin and α1-acid glycoprotein, and specific radioactivities were determined. The results indicated that the pathway of secretion of albumin and α1-acid glycoprotein was rough endoplasmic reticulum → smooth endoplasmic reticulum → Golgi complex → blood. Although there was little difference in the pathway or rate of secretion of the proteins under study in normal and experimental animals, there was an increase in specific radioactivities of labelled leucine and glucosamine associated with α1-acid glycoprotein when isolated from subcellular fractions from livers from experimental animals.

Purification of deoxyribonucleic acid polymerase .delta. from calf thymus: partial characterization of physical properties

Biochemistry ◽  
1980 ◽  
Vol 19 (10) ◽  
pp. 2096-2101 ◽  
Author(s):  
Marietta Y. W. Tsang Lee ◽  
Cheng-Keat Tan ◽  
Antero G. So ◽  
Kathleen M. Downey
Keyword(s):  
Physical Properties ◽  
Deoxyribonucleic Acid ◽  
Partial Characterization ◽  
Calf Thymus

scholarly journals Experimental Ehrlichia canis infection changes acute-phase proteins

2012 ◽  
Vol 21 (3) ◽  
pp. 206-212 ◽  
Author(s):  
Thiago Demarchi Munhoz ◽  
Joice Lara Maia Faria ◽  
Giovanni Vargas-Hérnandez ◽  
José Jurandir Fagliari ◽  
Áureo Evangelista Santana ◽  
...  
Keyword(s):  
Early Detection ◽  
Early Diagnosis ◽  
Acute Phase ◽  
Acute Phase Proteins ◽  
Ehrlichia Canis ◽  
Laboratory Findings ◽  
Early Detection Of Disease ◽  
Acid Glycoprotein ◽  
The Third ◽  
Canine Ehrlichiosis

Early diagnosis of canine ehrlichiosis favors prompt institution of treatment and improves the prognosis for the animal, since this disease causes mortality among dogs. Studies have shown that determining the concentration of acute-phase proteins (APPs) may contribute towards early detection of disease and aid in predicting the prognosis. This study aimed to evaluate the APP profile in dogs experimentally infected with Ehrlichia canis, at the start of the infection and after treatment. It also investigated whether any correlation between APP levels and the clinical and laboratory alterations over the course of the disease would be possible. The results obtained showed abnormal levels of all the APPs on the third day after infection (D3), with the highest levels being reached on D18, with the exception of ceruloplasmin and acid glycoprotein, which presented their peaks on D6 and D12 respectively. We concluded that assessment of APP levels could contribute towards establishing an early diagnosis of canine ehrlichiosis, particularly regarding acid glycoprotein and ceruloplasmin, since these proteins were detected at increased levels even before the onset of clinical and laboratory findings of the disease.

Detection and partial characterization of extracellular inducers of persistence in Staphylococcus epidermidis and Staphylococcus aureus

2021 ◽  
Vol 70 (6) ◽  
Author(s):  
Elyse C. Curry ◽  
Ryan G. Hart ◽  
Danni Y. Habtu ◽  
Neal R. Chamberlain
Keyword(s):  
Molecular Weight ◽  
Staphylococcus Aureus ◽  
Staphylococcus Epidermidis ◽  
Type Species ◽  
Proteinase K ◽  
Partial Characterization ◽  
Content Type ◽  
Link Type ◽  
Inducing Factors

Introduction. This study describes the identification and partial characterization of persistence-inducing factors (PIFs) from staphylococci. Hypothesis/Gap Statement. Increases in persisters during mid-log phase growth indicate that quorum-sensing factors might be produced by staphylococci. Aim. To identify and partially characterize PIFs from Staphylococcus epidermidis RP62A and Staphylococcus aureus SH1000. Methodology. Others have demonstrated a significant increase in persister numbers during mid-log phase. Inducers of this mid-log increase have yet to be identified in staphylococci. Optical density at 600 nm (OD600) was used instead of time to determine when persister numbers increased during logarithmic growth. Concentrated culture filtrates (CCFs) from S. epidermidis and S. aureus were obtained at various OD600s and following incubation at 16 h. The CCFs were used to develop a PIF assay. The PIF assay was used to partially characterize PIF from S. epidermidis and S. aureus for sizing of PIF activity, temperature and protease sensitivity and inter-species communications. Results. The optimal OD600s for S. epidermidis and S. aureus PIF assays were 2.0 and 0.5, respectively. The highest PIF activity for both species was from CCF following incubation overnight (16 h). S. epidermidis ’ PIF activity was decreased by storage at 4 oC but not at 20 oC (16 h), 37 oC (1 h) or 100 oC (15 min). S. aureus ’ PIF activity was decreased following storage at 4 oC (2 weeks) and after boiling at 100 oC for 5 min but not after incubation at 37 oC (1 h). PIF activity from both species went through a 3000 molecular weight cutoff ultrafilter. Proteinase K treatment of S. aureus PIF decreased activity but did not decrease the PIF activity of S. epidermidis . PIF from S. epidermidis did not increase persisters when used to treat S. aureus cells and nor did PIF from S. aureus increase persisters when used to treat S. epidermidis cells. Conclusions. Attempts to discover PIFs for staphylococci were unsuccessful due to the time-based means used to identify mid-log. Both staphylococcal species produce extracellular, low-molecular-weight inducers of persistence when assayed using an OD600 -based PIF assay.

scholarly journals Luminometric assays of seven acute-phase proteins in minimal volumes of serum, plasma, sputum, and bronchioalveolar lavage.

1986 ◽  
Vol 32 (5) ◽  
pp. 743-747 ◽  
Author(s):  
J Braun ◽  
T Schultek ◽  
K F Tegtmeier ◽  
A Florenz ◽  
C Rohde ◽  
...  
Keyword(s):  
Acute Phase ◽  
Acute Phase Proteins ◽  
Immunoglobulin A ◽  
C Reactive Protein ◽  
Acid Glycoprotein ◽  
Reactive Protein ◽  
Coefficients Of Variation ◽  
Alpha 1 Antitrypsin ◽  
Heel Prick ◽  
Secretory Immunoglobulin

Abstract We describe immunoluminometric assays for seven acute-phase proteins, which can be determined in minimal volumes of plasma, serum, sputum, and bronchioalveolar lavage. The theoretical volume of serum or plasma required to measure all seven analytes in duplicate is 130 nL, although in practice the smallest volume of sample was enough to fill a hematocrit tube (about 25 microL of blood), collected from neonates by the heel-prick method. The assays could be performed with 10 microL of sputum or with 100 microL of bronchioalveolar lavage. We measured alpha 1-antitrypsin, alpha 2-macroglobulin, alpha 1-acid glycoprotein, thyroxin-binding prealbumin, C-reactive protein, and total and secretory immunoglobulin A. The assays are rapid enough for all results to be returned to the ward on the same day and are suitable for monitoring neonatal sepsis. All coefficients of variation, derived from compound precision profiles, were less than 7% for clinically relevant analyte concentrations. Correlation with commercially available nephelometric assays was good.

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