scholarly journals Determination of the each fractional value of normal human serum protein by electrophoresis with use of the new cellulose acetate membrane; SEPARAX-SP. Comparative studies with the conventional membranes.

1991 ◽  
Vol 35 (5) ◽  
pp. 389-396
Author(s):  
Teruko Ohtake ◽  
Kimiko Tanaka ◽  
Masayo Noguchi ◽  
Shojiro Kano ◽  
Hisami Iri
1981 ◽  
Vol 27 (5) ◽  
pp. 736-738 ◽  
Author(s):  
J W Keyser ◽  
R Fifield ◽  
G L Watkins

Abstract When we compared four commercially available preparations of human serum albumin with the human serum standard IFCC 74/1 by radial immunodiffusion, by immunoprecipitation turbidimetry, by laser nephelometry, and by "rocket" immunoelectrophoresis, three of the preparations gave almost "theoretical" results with the immunoprecipitation turbidimetric method. Results by the other three methods tended inconsistently to be low. Four pools of normal human serum were also analyzed for albumin by these four immunochemical methods, again with IFCC 74/1 as the reference standard. The results were virtually identical with those obtained by fractionation with 1.8 mol/L sodium sulfate and determination of protein nitrogen in the filtrate. We suggest that a combination of (a) fractionation of a pool of normal human serum in this way and (b) critical comparison with selected commercial preparations of human serum albumin will permit standardization of the serum albumin determination.


1969 ◽  
Vol 15 (1) ◽  
pp. 42-55 ◽  
Author(s):  
Tetsuo Uete ◽  
Michiko Wasa ◽  
Akemi Shimogami

Abstract A simplified method for the determination of pepsinogen in blood and urine has been developed using serum protein as substrate. As crystalline pepsin digests human serum protein optimally in the region of pH 2, and blood exhibits such proteolytic activity on its own serum protein in this region, the determination of pepsinogen in blood is performed at this pH. The proteolytic activity of serum or plasma on its own (autologous) serum protein is inactivated by alkalinization. The blood of gastrectomized patients showed extremely low proteolytic activity in the region of pH 2 by the present method, indicating an absence of pepsinogen. The present method has greater specificity and accuracy than the method employing either hemoglobin or casein as substrate.


2014 ◽  
Vol 62 (1) ◽  
pp. 79-82 ◽  
Author(s):  
Yanjie Dong ◽  
Xuming Huang ◽  
Fang Wang ◽  
Junwei Wang ◽  
Hongyu Xia ◽  
...  

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