Abstract
We have examined the effect of conditioning the enzyme trypsin in solution at pH 8.2 in a large magnetic field before determining its reactivity towards a synthetic substrate N-benzoyl DL-arginine p-nitroanilide (BAPA). This “pretreatment” was allowed to proceed for as long as 3⅔ hr in a magnetic field of 208 kgauss at temperatures 26 and 36°C. No effect on reactivity was observed when such pretreated enzyme solutions were compared with identical but untreated enzyme solutions. A single such reaction, allowed to proceed directly in a magnetic field of 220 kgauss for 9 min, similarly showed no difference in rate from its control.
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Selected References
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- AKOYUNOGLOU G. EFFECT OF A MAGNETIC FIELD ON CARBOXYDISMUTASE. Nature. 1964 May 2;202:452–454. doi: 10.1038/202452a0. [DOI] [PubMed] [Google Scholar]
- ERLANGER B. F., KOKOWSKY N., COHEN W. The preparation and properties of two new chromogenic substrates of trypsin. Arch Biochem Biophys. 1961 Nov;95:271–278. doi: 10.1016/0003-9861(61)90145-x. [DOI] [PubMed] [Google Scholar]
- Maling J. E., Weissbluth M., Jacobs E. E. Enzyme substrate reactions in high magnetic fields. Biophys J. 1965 Nov;5(6):767–776. doi: 10.1016/S0006-3495(65)86751-0. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rabinovitch B., Maling J. E., Weissbluth M. Enzyme-substrate reactions in very high magnetic fields. I. Biophys J. 1967 Mar;7(2):187–204. doi: 10.1016/S0006-3495(67)86583-4. [DOI] [PMC free article] [PubMed] [Google Scholar]
