Sensitivity of adenylate kinase isozymes from normal and dystrophic human 
muscle to sulfhydryl reagents

Schirmer, R. Heiner; Thuma, Eva

doi:10.1016/0005-2744(72)90201-X

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Sensitivity of adenylate kinase isozymes from normal and dystrophic human muscle to sulfhydryl reagents

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Schirmer, R. Heiner
Max Planck Institute for Medical Research, Max Planck Society;

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Thuma, Eva
Max Planck Institute for Medical Research, Max Planck Society;

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http://www.sciencedirect.com/science/article/pii/000527447290201X/pdf?md5=283b3ea4f57b42dc449ef640a8598da1&pid=1-s2.0-000527447290201X-main.pdf
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Citation

Schirmer, R. H., & Thuma, E. (1972). Sensitivity of adenylate kinase isozymes from normal and dystrophic human muscle to sulfhydryl reagents. Biochimica et Biophysica Acta: BBA, 268(1), 92-97. doi:10.1016/0005-2744(72)90201-X.

Cite as: https://hdl.handle.net/11858/00-001M-0000-002D-8164-3

Abstract

1.|Crystalline human muscle adenylate kinase (ATP:AMP phosphotransferase, EC 2.7.4.3) possesses two sulfhydryl groups. The enzyme was only partially inactivated when these thiol groups were reacted with mercury or silver compounds. Reaction with Ellman's reagent, however, resulted in complete loss of activity.
2.

2.|The adenylate kinase activity of extracts of normal human muscle was inhibited by Ellman's reagent whereas the adenylate kinase activity of extracts of human liver was insensitive towards all sulfhydryl reagents.
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3.|In extracts of diseased human muscle (progressive muscular dystrophy Duchenne type) 40–60% of the adenylate kinase activity remained after treatment with Ellman's reagent.
4.

4.|These and other results indicate that the adenylate kinase isozymes might be an adequate system for investigating the role of SH-proteins in the pathogenesis of muscular dystrophies.
5.

5.|The reaction of mercury compounds with 2-nitro-5-thiobenzoate was used for the quantitative determination of organic mercurials.