scholarly journals CHEMICAL, CLINICAL, AND IMMUNOLOGICAL STUDIES ON THE PRODUCTS OF HUMAN PLASMA FRACTIONATION. I. THE CHARACTERIZATION OF THE PROTEIN FRACTIONS OF HUMAN PLASMA 12

1944 ◽  
Vol 23 (4) ◽  
pp. 417-432 ◽  
Author(s):  
Edwin J. Cohn ◽  
John L. Oncley ◽  
Laurence E. Strong ◽  
Walter L. Hughes ◽  
S. Howard Armstrong
Keyword(s):  
Human Plasma ◽  
Protein Fractions

scholarly journals Purification and characterization of an insulin-like growth factor II variant from human plasma

1989 ◽  
Vol 264 (32) ◽  
pp. 19155-19160 ◽  
Author(s):  
B Hampton ◽  
W H Burgess ◽  
D R Marshak ◽  
K J Cullen ◽  
J F Perdue
Keyword(s):  
Growth Factor ◽  
Human Plasma ◽  
Insulin Like Growth Factor ◽  
Purification And Characterization ◽  
Factor Ii

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 Development, Manufacturing and Characterization of a Highly Purified, Liquid Immunoglobulin G Preparation from Human Plasma

2014 ◽  
Vol 41 (3) ◽  
pp. 205-212 ◽  
Author(s):  
Inga A. Laursen ◽  
Lene Blou ◽  
John S. Sullivan ◽  
Peter Bang ◽  
Flemming Balstrup ◽  
...  
Keyword(s):  
Human Plasma ◽  
Immunoglobulin G

Heat Stable Human Plasma Protein Fractions Electrophoretically Rich in Albumin

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

scholarly journals Immunochemical characterization of human plasma fibronectin

1980 ◽  
Vol 191 (3) ◽  
pp. 719-727 ◽  
Author(s):  
M Vuento ◽  
E Salonen ◽  
K Salminen ◽  
M Pasanen ◽  
U K Stenman
Keyword(s):  
Human Plasma ◽  
Antigenic Structure ◽  
Antigenic Determinants ◽  
Proteolytic Degradation ◽  
Plasma Fibronectin ◽  
Native Protein ◽  
Covalent Interaction ◽  
Antigenic Activity ◽  
Haemagglutinating Activity

Human plasma fibronectin has been purified by a non-denaturing affinity chromatography procedure [Vuento & Vaheri, (1979) Biochem.J. 183, 331–337], and antisera have been raised by immunizing rabbits with the native protein. The antisera reacted strongly with native fibronectin, but only weakly with reduced and alkylated fibronectin or with heat-denaturated fibronectin. Denaturation also affected the haemagglutinating and gelatin-binding activities of fibronectin and increased its susceptibility to proteolytic degradation. The antisera reacted with fragments of fibronectin obtained by proteolysis with plasmin. Large fragments (mol.wt. 180000–200000), lacking the region harbouring the interchain disulphide bridges but containing the sites responsible for gelatin-binding and haemagglutinating activity, showed as intense a reaction with the antisera as intact fibronectin. Smaller peptides showed a weaker reaction. All fragments tested showed sensitivity to denaturation in their reaction with the antisera. The results were interpreted as showing that: (1) native fibronectin has an ordered conformation that is easily perturbed by denaturation; (2) most of the antigenic determinants of the protein are dependent on conformation; (3) the region of the fibronectin molecule containing the interchain disulphide bridges has only few antigenic determinants; and (4) covalent interaction of the two subunits does not contribute to the antigenic structure recognized by rabbit antisera. The observed correlation between the antigenic activity and a structural and functional intactness of fibronectin suggests that the antibodies to native fibronectin could be used as a conformational probe in studies on this protein.

CHARACTERIZATION OF SOLUBLE TRUNCATED FORMS OF THE AMYLOID PRECURSOR PROTEIN FROM HUMAN PLASMA

1990 ◽  
Vol 49 (3) ◽  
pp. 310
Author(s):  
M Schlossmacher ◽  
M Podlisny ◽  
A Mammen ◽  
R Barbour ◽  
M Palmert ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Human Plasma ◽  
Precursor Protein
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