Polarographische Eiweißuntersuchungen. VII. Das unterschiedliche Verhalten des Eiweißquotienten bei verschiedenen Eiweißarten

Tropp, Caspar; Geiger, Fritz; Stoye, Walter

doi:10.1515/bchm2.1943.277.4-6.192

Cited by 6 publications

(2 citation statements)

References 1 publication

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The double wave of various proteins ± egg albumen, pepsin, chymotrypsinogen, trypsin and insulin ± changes with pH in a similar way [84]: it starts increasing above pH 8, reaches its maximum between 9.3 and 10.3 and then falls to zero. The ratio of heights of the first to the second wave in the double wave changes with dilution ± the heights of the two waves exceeding each other on dilution has been called the ™crossing effect∫ [85]. When the concentration of ammonia in the solution is sufficiently increased, the double wave coalesces into a single one like in the solution of cysteine [80].…”

Section: Catalysis In Presence Of Cobalt Ions ± Brdicka Reactionmentioning

confidence: 99%

Early Polarographic Studies on Proteins

Heyrovský

2004

Electroanalysis

View full text Add to dashboard Cite

The first effects of proteins observed with the dropping mercury electrode were catalytic, due to evolution of hydrogen in weakly alkaline solutions. Catalytic lowering of hydrogen overvoltage in presence of cobalt ions, the socalled Brdicka reaction, became the main means for polarographic study of proteins. Apart from that, polarography has been used for following proteins in their adsorption on the electrode surface, in their anodic reaction with mercury at positive potentials, in reduction of the disulfidic bonds of their components, in their complexation with metallic ions in the solution, in electrode reactions of their prosthetic groups and in antigen-antibody interactions. Our review is limited to applications of the dropping mercury electrode.

show abstract