PROPERTIES OF VARIOUS ANTI-γ-GLOBULIN FACTORS IN HUMAN SERA

The serological and physicochemical properties of the following three forms of human anti-γ-globulin factors were compared: (a) rheumatoid factors; (b) Milgrom type anti-γ-globulin factors; and (c) factors directed against an antigen in human γG-globulin that is hidden in the intact molecule and revealed by enzymatic digestion at low pH. The property common to these factors is ability to interact with human γG-globulin; they are distinguishable because they react with different antigenic groups on this molecule. In all of five sera, the Milgrom type anti-γ-globulin factors were γM-globulins. They reacted with various human γG-globulin antibodies but failed to interact with γM-globulin type antibodies in agglutination and absorption experiments. When isolated from other anti-γ-globulin factors, they agglutinated red cells coated with intact anti-Rh antibodies, but failed to react with cells cells coated with pepsin-digested anti-Rh antibody. These observations indicate that the agglutinator reacts with the crystallizable, inert fragment of γG-globulin. Anti-γ-globulin activity directed against an antigen in human γG-globulin revealed by pepsin digestion was demonstrated in γG-, γA-, and γM-globulins. This anti-γ-globulin factor could be absorbed by antigen-antibody precipitates containing human antibody, which shows that the hidden antigen in human γG-globulin is revealed not only by enzymatic digestion at low pH, but also when γG-globulin is present as antibody in an antigen-antibody precipitate. Rheumatoid factors and Milgrom type anti-γ-globulin factors were also absorbed by antigen-antibody precipitates containing human antibody. The results indicate that the three distinct forms of antiγ-globulin factors may all be produced as a result of antigenic stimulation by autologous antigen-antibody complexes.

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Can keratin scaffolds be used for creating three-dimensional cell cultures?

Open Medicine ◽

10.1515/med-2020-0031 ◽

2020 ◽

Vol 15 (1) ◽

pp. 249-253

Author(s):

Marta Bochynska-Czyz ◽

Patrycja Redkiewicz ◽

Hanna Kozlowska ◽

Joanna Matalinska ◽

Marek Konop ◽

...

Keyword(s):

Cell Cultures ◽

Chemical Activation ◽

Three Dimensional ◽

Enzymatic Digestion ◽

Pepsin Digestion ◽

Cell Culturing ◽

3D Cell Cultures ◽

Associated Proteins ◽

Positive Effect ◽

Dimensional Cell

AbstractThree-dimensional (3D) cell cultures were created with the use of fur keratin associated proteins (F-KAPs) as scaffolds. The procedure of preparation F-KAP involves combinations of chemical activation and enzymatic digestion. The best result in porosity and heterogeneity of F-KAP surface was received during pepsin digestion. The F-KAP had a stable structure, no changes were observed after heat treatment, shaking and washing. The 0.15-0.5 mm fraction had positive effect for formation of 3D scaffolds and cell culturing. Living rat mesenchymal cells on the F-KAP with no abnormal morphology were observed by SEM during 32 days of cell culturing.

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Interactions between sphered human red cells in tube flow: Technique for measuring the strength of antigen-antibody bonds

Microvascular Research ◽

10.1016/0026-2862(82)90067-x ◽

1982 ◽

Vol 23 (2) ◽

pp. 231-238 ◽

Cited By ~ 5

Author(s):

Harry L. Goldsmith ◽

Phil Gold ◽

Joseph Shuster ◽

Koichi Takamura

Keyword(s):

Red Cells ◽

Tube Flow ◽

Antigen Antibody ◽

Human Red Cells

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Stimulation of the Potassium Transport System in Low Potassium Type Sheep Red Cells by a Specific Antigen Antibody Reaction

Nature ◽

10.1038/222477a0 ◽

1969 ◽

Vol 222 (5192) ◽

pp. 477-478 ◽

Cited By ~ 87

Author(s):

J. C. ELLORY ◽

ELIZABETH M. TUCKER

Keyword(s):

Transport System ◽

Specific Antigen ◽

Potassium Transport ◽

Red Cells ◽

Sheep Red Cells ◽

Low Potassium ◽

Antibody Reaction ◽

Antigen Antibody ◽

Stimulation Of

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THE EFFECT OF RHEUMATOID FACTORS AND OF ANTIGLOBULINS ON IMMUNE HEMOLYSIS IN VIVO

Journal of Experimental Medicine ◽

10.1084/jem.117.1.105 ◽

1963 ◽

Vol 117 (1) ◽

pp. 105-125 ◽

Cited By ~ 15

Author(s):

Manuel E. Kaplan ◽

James H. Jandl

Keyword(s):

Protein Content ◽

Blood Stream ◽

Body Fluids ◽

Red Cells ◽

Rheumatoid Factors ◽

Low Protein ◽

Immune Hemolysis

Studies were undertaken in man and in the rat comparing the effects of rheumatoid factors and immune antiglobulins on red cells sensitized with incomplete antibodies. The interaction of immune antiglobulins with sensitized red cells produced (a) agglutination in vitro and (b) an accelerated sequestration of the sensitized cells in vivo. In contrast, rheumatoid macroglobulins, although capable of agglutinating Rh-sensitized red cells in vitro, did not modify their destruction in vivo. The failure of rheumatoid factors to function as antiglobulins in vivo appears to reflect their non-reactivity with sensitized cells in whole serum. It is suggested: (a) that the native (7S) gamma globulins of plasma competitively inhibit rheumatoid factors from reacting with fixed antibody in the blood stream; (b) that if these macroglobulins do indeed have pathogenetic activity, this may be limited to body fluids of low protein content.

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Effects of Hydrothermal Treatments on Physicochemical Properties and In Vitro Digestion of Starch

Food Biophysics ◽

10.1007/s11483-021-09687-7 ◽

2021 ◽

Author(s):

Ishita Chakraborty ◽

Indira Govindaraju ◽

Sintu Rongpipi ◽

Krishna Kishore Mahato ◽

Nirmal Mazumder

Keyword(s):

Physicochemical Properties ◽

Water Solubility ◽

Amylose Content ◽

Potato Starch ◽

Brown Rice ◽

Food Products ◽

Enzymatic Digestion ◽

Diabetic Patients ◽

Degree Of Hydrolysis

AbstractStarchy food items such as rice and potato with high carbohydrate content raise blood sugar. Hence, consuming low glycaemic foods is one tool to keep diabetes under control. In this study, potato and brown rice (Njavara rice) starches were subjected to hydrothermal treatments: heat moisture treatment (HMT) and annealing (ANN) to develop starch-based food products fit for consumption by diabetic patients. The effects of hydrothermal treatments on physicochemical properties and in-vitro enzymatic digestion of starch were determined. It was observed that hydrothermal treatments decreased the swelling power (SP)% and increased the water solubility (WS)% of the native starches. Native potato starch (PSN) showed a high SP of 80.33%, while annealed potato starch (PANN) and heat moisture treated potato starch (PHMT) showed SP reduced to 65.33% and 51.66%, respectively. Similarly, the SP % reduced from 64.33% in native brown rice (BRN) to 44.66% in annealed brown rice (BRANN) and 38.33% in heat moisture treated brown rice (BRHMT). WS % increased from 32.86% in PSN to 36.66% in PANN and 40.66% in PHMT. In BRN, the WS % increased from 14.0% to 14.66% in BRANN and 18.33% in BRHMT. Amylose content increased from 13.23% and 14.56% in PSN and BRN to 16.14% in PANN 17.99% in PHMT, 17.33% in BRANN, and 18.98% in BRHMT. The PSN crystallinity index reduced from 33.49 to 30.50% in PANN and 32.60% in PHMT. At 12 h of enzymatic digestion, it was found that the degree of hydrolysis (DoH) of PHMT (31.66%) and PANN (36.82%) reduced when compared to PSN (41.09%). Similarly, BRHMT exhibited the lowest DoH at 12 h compared to BRANN (29.24%) and BRN (35.48%). This study highlights the importance of hydrothermal treatments on starch in developing low glycaemic index commercial starch-based food products.

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Leukocyte Antibodies in Human Sera and in Immune Rabbit Sera

Blood ◽

10.1182/blood.v12.11.953.953 ◽

1957 ◽

Vol 12 (11) ◽

pp. 953-971 ◽

Cited By ~ 22

Author(s):

ROY L. WALFORD ◽

E. TAYLOR PETERSON ◽

PATRICIA DOYLE

Keyword(s):

Antibody Formation ◽

Agar Plate ◽

Human Leukocyte ◽

Delayed Reaction ◽

Human Leukocytes ◽

Human Sera ◽

Set Up ◽

Antigen Antibody ◽

Leukocyte Antibody ◽

Immune Rabbit

Abstract A study of leukocyte antibodies is presented using (1) the sera of rabbits immunized with human leukocytes, and (2) the sera of three patients screened for the presence of such antibodies from among 36 patients with hematologic disease, 31 of whom (including the 3 studied in detail) had received multiple transfusions. The following technics are described and were employed: Leukoagglutination, leukoprecipitation including tube and agar-plate methods, agglutination of antigen-coated tanned and untanned sheep erythrocytes, the effect of antisera upon phagocytosis of heat-killed staphylococci by leukocytes, and upon ameboid motility of leukocytes. The leukoagglutinin test gives reliable clearcut results providing that appropriate controls are included and certain criteria adhered to, in order to facilitate the recognition of clumping due to other factors than true antigen-antibody union. No leukoprecipitins were detected in human sera with the technics used in this study. Immune rabbit sera, on the other hand, gave two reaction-lines in agar media, when set up against leukocyte extract. Immune rabbit sera reacted strongly with antigen-coated tanned sheep red blood cells. Human sera did not so react. One of the three selected human sera reacted with antigen-coated untanned erythrocytes, suggesting the presence of a polysaccharide antigen extractable from human leukocytes and capable of stimulating antibody formation in the human. Immune rabbit sera, and other human sera, did not react in this test. A suggestive but perhaps not a conclusive effect upon phagocytosis of bacteria by leukocytes exposed to human leukocyte antibody for 1 hour could be demonstrated. By means of ameboid motility studies, a cytotoxic effect of the human antisera upon human leukocytes could be demonstrated after 18 hours of incubation, but not after 3 hours. This was interpreted as evidence of a delayed reaction. Certain cardinal points from a clinical and theoretical standpoint with regard to the genesis of leukocyte antibodies in man are briefly reviewed. A possible analogy between leukocyte antibody formation and the homograft reaction is discussed. It is suggested that the rarity of leukocyte iso-antibody formation following transfusion is related to the fact that the intravenous pathway may be a poor route of immunization for these antigens.

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Dissociation of mannan--serum complexes and detection of Candida albicans mannan by enzyme immunoassay variations.

Clinical Chemistry ◽

10.1093/clinchem/28.2.306 ◽

1982 ◽

Vol 28 (2) ◽

pp. 306-310 ◽

Cited By ~ 23

Author(s):

E Reiss ◽

L Stockman ◽

R J Kuykendall ◽

S J Smith

Keyword(s):

Candida Albicans ◽

Enzyme Immunoassay ◽

Alkali Treatment ◽

Human Sera ◽

Normal Human ◽

Sandwich Enzyme Immunoassay ◽

Antigen Antibody ◽

Bead Method

Abstract Candida albicans mannan was added to normal human sera and the resulting complexes were dissociated by boiling (boil) with EDTA or by alkali treatment (bead method). The mannan released was detected by "sandwich" enzyme immunoassay (EIA) or by EIA inhibition. Each EIA took 2.3 h to perform. The total time for the boil-EIA combination was 2.7 h and for the bead-EIA, 3.8 h. The temperature favorable for antigen--antibody incubation was 4 degrees C. The sandwich EIAs were preferable to EIA inhibition because absorbance was directly proportional to mannan concentration, within-run variation was decreased, and accuracy was increased. The boil-sandwich EIA had the highest sensitivity in the 12.5 to 200 micrograms/L range.

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Rate nephelometric measurement of rheumatoid factor in serum.

Clinical Chemistry ◽

10.1093/clinchem/25.11.1909 ◽

1979 ◽

Vol 25 (11) ◽

pp. 1909-1914 ◽

Cited By ~ 16

Author(s):

P R Finley ◽

M J Hicks ◽

R J Williams ◽

J Hinlicky ◽

D A Lichti

Keyword(s):

Rheumatoid Factor ◽

Control Level ◽

Positive Control ◽

Standard Curve ◽

Graph Paper ◽

Rate Of Increase ◽

Human Sera ◽

Reference Preparation ◽

Level I ◽

Antigen Antibody

Abstract We describe the measurement of rheumatoid factor in human sera with a rate nephelometer. The National Reference Preparation for Rheumatoid Factors is used to calibrate the assay in International Units. We used Hyland Positive Control, Level I, as a secondary standard. The standard curve is exponential, but is linear when plotted on log-log graph paper. Aggregated immune globulin (IgG) is the antigen used to detect rheumatoid factor (IgM-class antibody to IgG). The rate reaction measures the rate of increase in light-scatter by the antigen-antibody complexes; the reaction takes place in 17 to 20 s. Precision, linearity, and accuracy are excellent. Results agree well with those for a commonly used latex precipitation test. The advantages of speed, quantification in International Units, and superior discrimination of concentration as compared to serological titration provide a more reliable test for use in the diagnosis and treatment of rheumatoid arthritis.

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