Company Filing History:
Years Active: 2015
Title: Innovations in Enzyme Activity Measurement by Hans Jörg Meier
Introduction
Hans Jörg Meier, an inventive mind from Constance, Germany, has made significant contributions to the field of enzymology. With a focus on innovative methods to assess enzyme activity, he has developed a patented solution that stands out in its unique approach to de-inhibition and measurement.
Latest Patents
Meier holds a patent for a groundbreaking method titled "Method for measuring the activity of cathepsin B after de-inhibition." This invention outlines a technique for accurately measuring enzyme activity in samples containing both enzymes and their corresponding inhibitors. By enabling the detection of enzymatic reactions through fluorescence, his method allows for precise quantification of enzyme activity by monitoring the concentration of reaction products over time. A notable aspect of this patent is the use of a rigid carrier for de-inhibiting the enzyme, showcasing inventive engineering in biochemical measurement techniques.
Career Highlights
Hans Jörg Meier is associated with Papst Licensing GmbH & Co. KG, where he continues to work on advancements in enzyme measurement technologies. His career is marked by dedication to enriching the scientific community through innovative methods that enhance research and clinical applications.
Collaborations
Working alongside Hans Werner Hofer, Meier has established a fruitful collaborative environment that fosters creativity and innovation in their projects. Their partnership has proven invaluable in refining their research approaches and expanding the technological capabilities available for enzyme measurements.
Conclusion
Hans Jörg Meier's contributions to the field of enzymology and his patented inventions provide critical advancements that benefit both research institutions and clinical applications. His work reflects a commitment to innovation and excellence, ensuring ongoing progress in the measurement of enzyme activities, particularly in the context of cathepsin B.
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