scholarly journals Determination of the subunit composition of haptoglobin 2-1 polymers using quantitative densitometry of polyacrylamide gels.

1976 ◽  
Vol 251 (19) ◽  
pp. 5845-5851
Author(s):  
D C Hooper ◽  
A C Peacock
1973 ◽  
Vol 51 (11) ◽  
pp. 2217-2222 ◽  
Author(s):  
R. B. van Huystee

The prime purpose of this proteolysis study was to direct attention to alternate means of measuring proteolytic activity other than the determination of free amino acids. The release of peptides from a macromolecular protein during incubation with either papain, pronase, or trypsin was determined by measuring the presence of 280-nm-absorbing molecules in the fractionation range of Sephadex G 25 eluant after incubation. The formation of larger proteinaceous constituents by proteolysis of arachin was analyzed by disc electrophoresis on polyacrylamide gels. Using these techniques it was noted that papain was the most efficient proteolytic agent for the degradation of arachin.


1991 ◽  
Vol 12 (12) ◽  
pp. 1045-1050 ◽  
Author(s):  
Hein A. Van Lith ◽  
Manuela Haller ◽  
Bert F. M. Van Zutphen ◽  
Anton C. Beynen

2021 ◽  
pp. 303-315
Author(s):  
Jorge Juárez ◽  
María del Rayo Graciela Guevara-Villa ◽  
Anabel Sánchez-Sánchez ◽  
Raquel Díaz-Hernández ◽  
Leopoldo Altamirano-Robles

1978 ◽  
Vol 171 (1) ◽  
pp. 79-82 ◽  
Author(s):  
P L Storring ◽  
R J Tiplady

A simple method is described for the determination of polypeptides and proteins in polyacrylamide gels after isoelectric focusing. Precipitates formed in trichloroacetic acid, under controlled conditions, are quantified densitometrically by measuring the proportion of light scattered. The procedure is of particular value in its applicability to smaller polypeptides, with mol.wts. of 3000-6000, which are not fixed adequately in gels by other procedures currently in use. The working range, over which polypeptide concentration is proportional to the effective absorbance, is approx. 1-30 microgram per component.


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