Biological and immunological characterization of inhibin forms in human plasma

1996 ◽  
Vol 81 (2) ◽  
pp. 669-676 ◽  
Author(s):  
D. Robertson
Keyword(s):  
Human Plasma ◽  
Immunological Characterization

scholarly journals The immunological characterization of several human ribonucleases by using primary binding tests

1977 ◽  
Vol 163 (3) ◽  
pp. 419-426 ◽  
Author(s):  
E A Neuwelt ◽  
M Schmukler ◽  
M S Niziak ◽  
P B Jewett ◽  
C C Levy
Keyword(s):  
Human Plasma ◽  
Cross Reaction ◽  
The Other ◽  
Human Pancreas ◽  
Human Tissues ◽  
Antigenic Difference ◽  
Immunological Characterization ◽  
Similarities And Differences

RNAases (ribonucleases), purified from four human tissues, as well as bovine pancreatic RNAase (RNAase A), were studied by immunodiffusion methods and by two different primary binding tests. The enzymes fell into two groups immunologically, those purified from plasma and pancreas in one and those from spleen and liver in the other. No antigenic cross-reaction between the two groups was detected by any of the immunoassays used. There was a slight antigenic cross-reaction between the human and bovine pancreatic RNAases. The liver and spleen RNAases were immunologically identical by all criteria used, whereas a small but consistent antigenic difference between the human plasma and human pancreas enzymes was detected. The significance of this difference between the human plasma and pancreas RNAases is discussed in relation to similarities and differences in their properties.

scholarly journals Immunological characterization of human liver α-D-mannosidase

1975 ◽  
Vol 151 (3) ◽  
pp. 469-475 ◽  
Author(s):  
N Phillips ◽  
D Robinson ◽  
B Winchester
Keyword(s):  
Human Brain ◽  
Human Plasma ◽  
Human Liver ◽  
Double Diffusion ◽  
Immunological Characterization ◽  
Precipitin Line ◽  
Structural Resemblance ◽  
Optimum Ph

Antiserum was raised against purified human liver α-D-mannosidase B. It precipitated α-mannosidases A and B from solution, demonstrating the close structural resemblance of these 2 forms of acidic α-mannosidase activity. A continuous enzymically active precipitin line with no spurs was obtained when α-mannosidase A and B were placed in adjacent wells on Ouchterlony double-diffusion plates. The antiserum precipitated acidic but not neutral α-mannosidase from an extract of human liver, confirming that the acidic and neutral activities are not closely related. Acidic activity was also precipitated from extracts of human brain, kidney and leucocytes by the antiserum. However, it did not cross-react with bovine acidic α-mannosidase activity or with the activity in human plasma that has an optimum pH of 5.5. The two acidic forms of human liver α-mannosidase, A and B, are immunologically identical but distinct from neutral α-mannosidase and that activity with an optimum pH of 5.5.

Biological and immunological characterization of inhibin forms in human plasma.

1996 ◽  
Vol 81 (2) ◽  
pp. 669-676
Author(s):  
D Robertson ◽  
H G Burger ◽  
J Sullivan ◽  
N Cahir ◽  
N Groome ◽  
...  
Keyword(s):  
Human Plasma ◽  
Immunological Characterization

The Immunological Characterization of Human Antibodies to Factor VIII Isolated by Immuno-Affinity Chromatography

1981 ◽  
Vol 45 (01) ◽  
pp. 060-064 ◽  
Author(s):  
M L Kavanagh ◽  
C N Wood ◽  
J F Davidson
Keyword(s):  
Factor Viii ◽  
Affinity Chromatography ◽  
Gel Filtration ◽  
Immunological Characterization ◽  
Human Antibodies ◽  
Heavy Chains ◽  
Light Chain Type ◽  
Antibody Preparations ◽  
Chain Type

SummaryNine human antibodies to factor VIII were isolated from haemophilic plasmas by affinity chromatography and gel filtration and six were subsequently subjected to immunological characterization. Three partially purified preparations were similarly characterized. Eight of the antibodies were characterized as being exclusively IgG and one preparation was found to contain IgM. Seven of the antibodies contained only a single light chain type, four being of type lambda and three of type kappa. Two antibody preparations contained both kappa and lambda light chains. In four of the preparations, only a single heavy chain sub-class could be demonstrated, three of IgG3 and one of IgG4. Of the remainder, three were a mixture of IgG3 and IgG4 sub-classes and one contained both IgG2 and IgG4. IgG sub-classification could not be achieved with the IgM-containing preparation. These results demonstrate a restricted heterogeneity of light and heavy chains in human antibodies to factor VIII.

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