Renate Wieninger-Rustemeyer

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The activity of trypsin was determined by using N alpha-Benzoyl-L-arginin-p-nitroanilid (L-BAPA) as a substrate, and adding either the elements Cu, Zn, Fe, Ni, and Co alone or in combination with copper in the concentration range of 0.9 x 10(-7) to 0.9 x 10(-4) moles Men+/l. Cu and Zn don't elevate the activity of trypsin but if they are added separately in(More)
In vivo experiments with Sprague-Dawley rats were conducted in order to explore the influence of Cu2+, Zn2+ as well as of the combinations of both on the activity of trypsin. The solutions of the trace elements were given per os, the animals were killed 30 min after the applications, and the activity of trypsin was determined in the juice of the small(More)
In vitro experiments were conducted with trypsin and Na-Benzoyl-l-arginine-p-nitroanilid (L-BAPA) as substrate. The aim of the work was to explore the influence of additional Cu2+, Zn2+, Co2+, Ni2+ and Fe3+ ions in the reaction mixtures on the trypsin activity at different enzyme-substrate ratios (E : S = 1 : 100; 1 : 50; 1 : 10; 1 : 5). The reaction(More)
In vitro experiments were carried out in order to investigate the influence of Cu++-ions on the tryptic hydrolysis of casein and soybean protein. The admixture of 10(-3) to 10(-2) Mol Cu++/l to the reaction preparations results in the activation of trypsin in both substrates. The further increase of the Cu++-concentration results in a decrease of the(More)
The rate of hydrolysis of the synthetic trypsin substrate N alpha-benzoyl-L-arginine-p-nitroanilide was determined from turnover rate curves, when the trace elements zinc, iron, cobalt, and nickel were added in the concentration range from 0.9 . 10(-7) to 0.9 . 10(-3) mol Men+/l. The enzyme substrate ratio was 1:50. An influence on the activity of trypsin,(More)
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